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Conserved domains on  [gi|489522574|ref|WP_003427360|]
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BglG family transcription antiterminator LicT [Clostridioides difficile]

Protein Classification

Bg1G family transcriptional antiterminator( domain architecture ID 1004078)

Bg1G family transcriptional antiterminator similar to Dickeya chrysanthemi beta-glucoside operon antiterminator that mediates the positive regulation of the beta-glucoside (arb) operon by functioning as a transcriptional antiterminator

CATH:  1.10.1790.10
Gene Ontology:  GO:0045893|GO:0003723

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09772 super family cl31605
transcriptional antiterminator BglG; Provisional
 1-277 1.68e-69

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.11  E-value: 1.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574   1 MIINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISNKLQELLNNIPIEHMKLSSEIIEY 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  81 AQIKLNKkLNESIYISLSDHTYSAIQRMKEGINVKNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 161 VNAQLSEGHTLASDITKLIQEVLSIVRYHFRIEFHEESVFYYRFIMHLKFFAQRlLLDSAHKGETDKELLSIIKSKYNKE 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWR-ILEHASINDSDESLQQAVKQNYPQA 240

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489522574 241 FECVVKIKNFIKKQYNYILTDDELICLTIHLAKVVKD 277
Cdd:PRK09772 241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-277 1.68e-69

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.11  E-value: 1.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574   1 MIINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISNKLQELLNNIPIEHMKLSSEIIEY 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  81 AQIKLNKkLNESIYISLSDHTYSAIQRMKEGINVKNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 161 VNAQLSEGHTLASDITKLIQEVLSIVRYHFRIEFHEESVFYYRFIMHLKFFAQRlLLDSAHKGETDKELLSIIKSKYNKE 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWR-ILEHASINDSDESLQQAVKQNYPQA 240

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489522574 241 FECVVKIKNFIKKQYNYILTDDELICLTIHLAKVVKD 277
Cdd:PRK09772 241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
62-272 1.16e-38

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 143.08  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  62 LLNNIPIEHMKLSSEIIEYAQIKLNKKLNESIYISLSDHTYSAIQRMKEGINVK--NAILWEIKRfyKEEFEIGMKALDI 139
Cdd:COG3711  170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 140 IENKTGIKLPEDEAGFIAFHIVNAQLSEGHTLAS----DITKLIQEVLSIVRYHFRIEFHEESVFYYRFIMHLKFFAQRL 215
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGARLNNDNELSEiitlEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489522574 216 LldsaHKGETDKELLSIIKSKYNKEFECVVKIKNFIKKQYNYILTDDELICLTIHLA 272
Cdd:COG3711  328 K----YGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFG 380
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 1.50e-20

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 215004  Cd Length: 55  Bit Score: 82.52  E-value: 1.50e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489522574     1 MIINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEI 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-57 1.86e-19

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 460815  Cd Length: 56  Bit Score: 79.78  E-value: 1.86e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489522574    2 IINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISN 57
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-277 1.68e-69

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.11  E-value: 1.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574   1 MIINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISNKLQELLNNIPIEHMKLSSEIIEY 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  81 AQIKLNKkLNESIYISLSDHTYSAIQRMKEGINVKNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 161 VNAQLSEGHTLASDITKLIQEVLSIVRYHFRIEFHEESVFYYRFIMHLKFFAQRlLLDSAHKGETDKELLSIIKSKYNKE 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWR-ILEHASINDSDESLQQAVKQNYPQA 240

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489522574 241 FECVVKIKNFIKKQYNYILTDDELICLTIHLAKVVKD 277
Cdd:PRK09772 241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
62-272 1.16e-38

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 143.08  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  62 LLNNIPIEHMKLSSEIIEYAQIKLNKKLNESIYISLSDHTYSAIQRMKEGINVK--NAILWEIKRfyKEEFEIGMKALDI 139
Cdd:COG3711  170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 140 IENKTGIKLPEDEAGFIAFHIVNAQLSEGHTLAS----DITKLIQEVLSIVRYHFRIEFHEESVFYYRFIMHLKFFAQRL 215
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGARLNNDNELSEiitlEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489522574 216 LldsaHKGETDKELLSIIKSKYNKEFECVVKIKNFIKKQYNYILTDDELICLTIHLA 272
Cdd:COG3711  328 K----YGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFG 380
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 1.50e-20

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 215004  Cd Length: 55  Bit Score: 82.52  E-value: 1.50e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489522574     1 MIINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEI 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-57 1.86e-19

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 460815  Cd Length: 56  Bit Score: 79.78  E-value: 1.86e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489522574    2 IINKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISN 57
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-163 1.21e-18

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 78.45  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574   76 EIIEYAQIKLNKKL-NESIYISLSDHTYSAIQRMKEGINVKNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAG 154
Cdd:pfam00874   2 EIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 489522574  155 FIAFHIVNA 163
Cdd:pfam00874  82 YIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
27-164 8.33e-15

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 74.38  E-value: 8.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  27 KGIGYQKSKGNLIDKTKVNKVFRISNKEISNKLQELLNNIPIEHMKLSSEIIEYAQIKLNKKLNESIYISLSDHTYSAIQ 106
Cdd:COG3933  414 LGIDEEEINIIIEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIE 493

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489522574 107 RMKEGINVKNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHIVNAQ 164
Cdd:COG3933  494 RIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLN 551
BglG COG3711
Transcriptional antiterminator [Transcription];
57-160 7.07e-12

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 65.27  E-value: 7.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  57 NKLQELLNNIPIEHMKLSSEIIEYAQIKLNKKLNES--IYISLSDHTYSAIQRMKEGINVKNAILWEIKRFYKEEFEIGM 134
Cdd:COG3711  274 NNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDslLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAK 353

                         90       100
                 ....*....|....*....|....*.
gi 489522574 135 KALDIIENKTGIKLPEDEAGFIAFHI 160
Cdd:COG3711  354 KIAKYLEKELGIEIPEDEIGYLTLHF 379
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 180-271 4.91e-10

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 55.34  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  180 QEVLSIVRYHFRIEFHEESvFYYRFIMHLKFFAQRLlldsaHKGETDK-ELLSIIKSKYNKEFECVVKIKNFIKKQYNYI 258
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDI-LYIRLILHLAFAIERI-----KEGITIEnPLLEEIKEKYPKEFEIAKKILEILEEELGIE 74

                          90
                  ....*....|...
gi 489522574  259 LTDDELICLTIHL 271
Cdd:pfam00874  75 LPEDEIGYIALHF 87
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 37-167 6.44e-07

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 50.49  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  37 NLIDKTKVNKVFR--ISNKEISNKLQELLNNIPIEHMKLSSEIIEYAQIKLNKKLNESIYISLSDHTYSAIQRMKEGINV 114
Cdd:COG1221  435 NKIISKDIESYFKklIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKI 514

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489522574 115 KNAILWEIKRFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHIVNAQLSE 167
Cdd:COG1221  515 INPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLLIELKEEK 567
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
3-280 3.46e-05

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 45.11  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574   3 INKILNNNVVITLDDNDEEVIVMGKGIGYQKSKGNLIDKTKVNKVFRISNKEISNKLQELLNNIPIEHMKLSSEIIEYAQ 82
Cdd:COG3933  289 EFEEEEIRIIKILIVLLLALLLLLLYVNNLGQLGLLKLLIKAAAAAALAKAIKEATIILRLLSKLLKLLLLLLLNERLLL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574  83 IKLNKKLNESIYISLSDHTYSAIQRMKEGINVKNAILweikrFYKEEFEIGMKALDIIENKTGIKLPEDEAGFIAFHIVN 162
Cdd:COG3933  369 LELKILIEPLDIFFDSSASSDESDESEEDENLYEIIE-----IKKKLLLELGIDEEEINIIIEIDIDVHLLKFIYDDNKN 443

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489522574 163 AQLSE-GHTLASDITKLIQEVLSIVRYHFRIEFHEEsvFYYRFIMHLKFFAQRLLLDSahkgETDKELLSIIKSKYNKEF 241
Cdd:COG3933  444 FNKEElAKIVDEDIINVVEEILELAEKKLGRKFSEN--FIYALSLHLSSFIERIKEGK----EIINPNLNEIKKKYPKEF 517

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489522574 242 ECVVKIKNFIKKQYNYILTDDELICLTIHLAKVVKDSNM 280
Cdd:COG3933  518 KVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNES 556
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 151-197 1.44e-03

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 460730 [Multi-domain]  Cd Length: 99  Bit Score: 37.33  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489522574  151 DEAGFIAFHIVNAQLSEGHTL---------ASDITKLIQEVLSIVRYHFRIEFHEE 197
Cdd:pfam02873  40 EQAGLKGYRIGGAQVSEKHANflvntggatAADVLALIEEVRERVKEKFGVELEPE 95
 
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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