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Conserved domains on  [gi|2635381164|ref|WP_321930713|]
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FCD domain-containing protein [Paraburkholderia guartelaensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
phnR_burk super family cl31336
phosphonate utilization associated transcriptional regulator; This family of proteins are ...
2-197 4.79e-62

phosphonate utilization associated transcriptional regulator; This family of proteins are members of the GntR family (pfam00392) containing an N-terminal helix-turn-helix (HTH) motif. This clade is found adjacent to or inside of operons for the degradation of 2-aminoethylphosphonate (AEP) in Polaromonas, Burkholderia, Ralstonia and Verminephrobacter.


The actual alignment was detected with superfamily member TIGR03338:

Pssm-ID: 132381 [Multi-domain]  Cd Length: 212  Bit Score: 192.68  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   2 QREIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALS 81
Cdd:TIGR03338  17 QDEIERAILSGELPPGAKLNESDIAARLGVSRGPVREAFRALEEAGLVRNEKNRGVFVREISLAEADEIYELRAVLDEIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  82 ASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFHLFRVHGLVQRGAL 161
Cdd:TIGR03338  97 GRRLAARITPTQLKVLKGLLDAMEDAAKAKDADRYARLNLRFHDALVEHAGNNKLTDTYRRLVKELSLFRRAALADGGAM 176
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2635381164 162 LESNAEHREIVAALKAKDAELSYRASFGHVSRGKER 197
Cdd:TIGR03338 177 AVSAAEHRAIVDAIASGDAERAGALMRAHVAASRER 212
 
Name Accession Description Interval E-value
phnR_burk TIGR03338
phosphonate utilization associated transcriptional regulator; This family of proteins are ...
2-197 4.79e-62

phosphonate utilization associated transcriptional regulator; This family of proteins are members of the GntR family (pfam00392) containing an N-terminal helix-turn-helix (HTH) motif. This clade is found adjacent to or inside of operons for the degradation of 2-aminoethylphosphonate (AEP) in Polaromonas, Burkholderia, Ralstonia and Verminephrobacter.


Pssm-ID: 132381 [Multi-domain]  Cd Length: 212  Bit Score: 192.68  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   2 QREIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALS 81
Cdd:TIGR03338  17 QDEIERAILSGELPPGAKLNESDIAARLGVSRGPVREAFRALEEAGLVRNEKNRGVFVREISLAEADEIYELRAVLDEIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  82 ASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFHLFRVHGLVQRGAL 161
Cdd:TIGR03338  97 GRRLAARITPTQLKVLKGLLDAMEDAAKAKDADRYARLNLRFHDALVEHAGNNKLTDTYRRLVKELSLFRRAALADGGAM 176
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2635381164 162 LESNAEHREIVAALKAKDAELSYRASFGHVSRGKER 197
Cdd:TIGR03338 177 AVSAAEHRAIVDAIASGDAERAGALMRAHVAASRER 212
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
3-203 3.53e-54

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 172.80  E-value: 3.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   3 REIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALSA 82
Cdd:COG1802    18 EALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAPLSPEEIRELYEVRAALEGLAA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  83 SLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFHLFRVHGLVQRGALL 162
Cdd:COG1802    98 RLAAERATPADLARLRALLEELEAAAAAGDVAAYLELDREFHRALVEAAGNPRLAELLRRLRARLRRYRRLSLRSPGRLE 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2635381164 163 ESNAEHREIVAALKAKDAELSYRASFGHVSRGKERMLVSLD 203
Cdd:COG1802   178 ESLAEHRAILDALEAGDAEAAAAALRAHLERARERLLEALA 218
FCD pfam07729
FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR ...
69-186 1.61e-18

FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR family. This domain binds to a range of effector molecules, including Lactate, Zn(II), Ni(II), Ca(II), Mg(II), citrate, sugar acids, sialic acid and N-acetylglucosamine-6-P, that regulate the transcription of genes through the action of the N-terminal DNA-binding domain pfam00392 (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). This domain is found in Swiss:P45427 and Swiss:P31460 that are regulators of sugar biosynthesis operons. It is also in the known structure of FadR where it binds to acyl-coA, the domain is alpha helical. This family has been named as FCD for (FadR C-terminal Domain).


Pssm-ID: 429623 [Multi-domain]  Cd Length: 121  Bit Score: 77.79  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  69 EVYDLRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFH 148
Cdd:pfam07729   1 ELYELRAALEPLAARLAAERATDEDLAELEALLEALEAAADAGDLEAFAEADREFHLALAEAAGNPVLARMLESLWDRLR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2635381164 149 LFRVHGLVQRGALLESNAEHREIVAALKAKDAELSYRA 186
Cdd:pfam07729  81 RLRRLLLSSPGRLRASLEEHRAILDAIRARDPEAARAA 118
FCD smart00895
This entry represents the C-terminal ligand binding domain of many members of the GntR family; ...
69-193 2.76e-16

This entry represents the C-terminal ligand binding domain of many members of the GntR family; This domain probably binds to a range of effector molecules that regulate the transcription of genes through the action of the N-terminal DNA-binding domain. This domain is found in and that are regulators of sugar biosynthesis operons. Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR after the Bacillus subtilis repressor of the gluconate operon. In general, these proteins contain a DNA-binding HTH domain at the N terminus, and an effector binding or oligomerisation domain at the C terminus. The winged-helix DNA-binding domain is well conserved in structure for the whole of the GntR family, and is similar in structure to other transcriptional regulator families. The C-terminal effector-binding and oligomerisation domains are more variable and are consequently used to define the subfamilies. Based on the sequence and structure of the C-terminal domains, the GtnR family can be divided into four major groups, as represented by FadR, HutC, MocR and YtrA, as well as some minor groups such as those represented by AraR and PlmA.


Pssm-ID: 214892 [Multi-domain]  Cd Length: 123  Bit Score: 72.01  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   69 EVYDLRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKGD-FAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEF 147
Cdd:smart00895   1 ELYEVRRALEPLAARLAAERATDEDLAALEALLDAMEAAAAAGDdLEEFAELDREFHRALAEAAGNPVLLELLESLRARL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2635381164  148 HLFRVHGLVQRGALLEsnaEHREIVAALKAKDAELSYRASFGHVSR 193
Cdd:smart00895  81 RRLRRLSLEAARRALD---EHRAILDAIRARDAEAARAAMREHLEA 123
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
3-60 1.35e-14

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 65.93  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2635381164   3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIK 60
Cdd:cd07377     8 DQLREAILSGELKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
PRK11414 PRK11414
GntR family transcriptional regulator;
12-183 1.44e-10

GntR family transcriptional regulator;


Pssm-ID: 183126 [Multi-domain]  Cd Length: 221  Bit Score: 58.73  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  12 GELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALSASLLAPMLTQ 91
Cdd:PRK11414   27 GALKPGARLITKNLAEQLGMSITPVREALLRLVSVNALSVAPAQAFTVPEVSKRQLDEINRIRYELELMAVALAVENLTP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  92 EMAGQLERYVDDMQDAAEKGDFAHFDPLN----LEFHDYIVRSTGNSRLIRLYRAFVKEFHLfrVHGLVQRGALLESNAE 167
Cdd:PRK11414  107 QDLAELQELLEKLQQAQEKGDMEQIINANrlfrLAIYHRSNMPILCEMIEQLWVRMGPSLHY--LYEAINPAELREHIEN 184
                         170
                  ....*....|....*.
gi 2635381164 168 HREIVAALKAKDAELS 183
Cdd:PRK11414  185 YRLLLAALKAKDKEGC 200
 
Name Accession Description Interval E-value
phnR_burk TIGR03338
phosphonate utilization associated transcriptional regulator; This family of proteins are ...
2-197 4.79e-62

phosphonate utilization associated transcriptional regulator; This family of proteins are members of the GntR family (pfam00392) containing an N-terminal helix-turn-helix (HTH) motif. This clade is found adjacent to or inside of operons for the degradation of 2-aminoethylphosphonate (AEP) in Polaromonas, Burkholderia, Ralstonia and Verminephrobacter.


Pssm-ID: 132381 [Multi-domain]  Cd Length: 212  Bit Score: 192.68  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   2 QREIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALS 81
Cdd:TIGR03338  17 QDEIERAILSGELPPGAKLNESDIAARLGVSRGPVREAFRALEEAGLVRNEKNRGVFVREISLAEADEIYELRAVLDEIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  82 ASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFHLFRVHGLVQRGAL 161
Cdd:TIGR03338  97 GRRLAARITPTQLKVLKGLLDAMEDAAKAKDADRYARLNLRFHDALVEHAGNNKLTDTYRRLVKELSLFRRAALADGGAM 176
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2635381164 162 LESNAEHREIVAALKAKDAELSYRASFGHVSRGKER 197
Cdd:TIGR03338 177 AVSAAEHRAIVDAIASGDAERAGALMRAHVAASRER 212
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
3-203 3.53e-54

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 172.80  E-value: 3.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   3 REIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALSA 82
Cdd:COG1802    18 EALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAPLSPEEIRELYEVRAALEGLAA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  83 SLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFHLFRVHGLVQRGALL 162
Cdd:COG1802    98 RLAAERATPADLARLRALLEELEAAAAAGDVAAYLELDREFHRALVEAAGNPRLAELLRRLRARLRRYRRLSLRSPGRLE 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2635381164 163 ESNAEHREIVAALKAKDAELSYRASFGHVSRGKERMLVSLD 203
Cdd:COG1802   178 ESLAEHRAILDALEAGDAEAAAAALRAHLERARERLLEALA 218
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
3-203 3.79e-33

DNA-binding transcriptional regulator, FadR family [Transcription];


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 119.27  E-value: 3.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAI------------- 68
Cdd:COG2186    14 EQLRELILSGELKPGDRLpSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSPWALLdplalllalddas 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  69 --EVYDLRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEkgDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKE 146
Cdd:COG2186    94 lrDLLEARLALEPEAARLAAERATDEDLARLEAALAEMEAAAD--DGEAFAEADLAFHRAIAEASGNPLLALLLESLREL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2635381164 147 FHLFRVHGLVQRGALLESNAEHREIVAALKAKDAELSYRASFGHVSRGKERMLVSLD 203
Cdd:COG2186   172 LRRSVRLTLRSPEARERSLAEHRAILDAIRAGDPEAARAAMRAHLEAVRERLREALA 228
FCD pfam07729
FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR ...
69-186 1.61e-18

FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR family. This domain binds to a range of effector molecules, including Lactate, Zn(II), Ni(II), Ca(II), Mg(II), citrate, sugar acids, sialic acid and N-acetylglucosamine-6-P, that regulate the transcription of genes through the action of the N-terminal DNA-binding domain pfam00392 (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). This domain is found in Swiss:P45427 and Swiss:P31460 that are regulators of sugar biosynthesis operons. It is also in the known structure of FadR where it binds to acyl-coA, the domain is alpha helical. This family has been named as FCD for (FadR C-terminal Domain).


Pssm-ID: 429623 [Multi-domain]  Cd Length: 121  Bit Score: 77.79  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  69 EVYDLRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEFH 148
Cdd:pfam07729   1 ELYELRAALEPLAARLAAERATDEDLAELEALLEALEAAADAGDLEAFAEADREFHLALAEAAGNPVLARMLESLWDRLR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2635381164 149 LFRVHGLVQRGALLESNAEHREIVAALKAKDAELSYRA 186
Cdd:pfam07729  81 RLRRLLLSSPGRLRASLEEHRAILDAIRARDPEAARAA 118
FCD smart00895
This entry represents the C-terminal ligand binding domain of many members of the GntR family; ...
69-193 2.76e-16

This entry represents the C-terminal ligand binding domain of many members of the GntR family; This domain probably binds to a range of effector molecules that regulate the transcription of genes through the action of the N-terminal DNA-binding domain. This domain is found in and that are regulators of sugar biosynthesis operons. Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR after the Bacillus subtilis repressor of the gluconate operon. In general, these proteins contain a DNA-binding HTH domain at the N terminus, and an effector binding or oligomerisation domain at the C terminus. The winged-helix DNA-binding domain is well conserved in structure for the whole of the GntR family, and is similar in structure to other transcriptional regulator families. The C-terminal effector-binding and oligomerisation domains are more variable and are consequently used to define the subfamilies. Based on the sequence and structure of the C-terminal domains, the GtnR family can be divided into four major groups, as represented by FadR, HutC, MocR and YtrA, as well as some minor groups such as those represented by AraR and PlmA.


Pssm-ID: 214892 [Multi-domain]  Cd Length: 123  Bit Score: 72.01  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   69 EVYDLRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKGD-FAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEF 147
Cdd:smart00895   1 ELYEVRRALEPLAARLAAERATDEDLAALEALLDAMEAAAAAGDdLEEFAELDREFHRALAEAAGNPVLLELLESLRARL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2635381164  148 HLFRVHGLVQRGALLEsnaEHREIVAALKAKDAELSYRASFGHVSR 193
Cdd:smart00895  81 RRLRRLSLEAARRALD---EHRAILDAIRARDAEAARAAMREHLEA 123
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
3-60 1.35e-14

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 65.93  E-value: 1.35e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2635381164   3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIK 60
Cdd:cd07377     8 DQLREAILSGELKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
4-59 2.19e-11

Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 57.24  E-value: 2.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2635381164   4 EIERMILSGELAPGQRLN-EKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFI 59
Cdd:pfam00392   8 RLREDILSGRLRPGDKLPsERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
3-59 3.29e-11

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 56.81  E-value: 3.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2635381164    3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFI 59
Cdd:smart00345   3 ERLREDIVSGELRPGDKLpSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
PRK11414 PRK11414
GntR family transcriptional regulator;
12-183 1.44e-10

GntR family transcriptional regulator;


Pssm-ID: 183126 [Multi-domain]  Cd Length: 221  Bit Score: 58.73  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  12 GELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTALSASLLAPMLTQ 91
Cdd:PRK11414   27 GALKPGARLITKNLAEQLGMSITPVREALLRLVSVNALSVAPAQAFTVPEVSKRQLDEINRIRYELELMAVALAVENLTP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  92 EMAGQLERYVDDMQDAAEKGDFAHFDPLN----LEFHDYIVRSTGNSRLIRLYRAFVKEFHLfrVHGLVQRGALLESNAE 167
Cdd:PRK11414  107 QDLAELQELLEKLQQAQEKGDMEQIINANrlfrLAIYHRSNMPILCEMIEQLWVRMGPSLHY--LYEAINPAELREHIEN 184
                         170
                  ....*....|....*.
gi 2635381164 168 HREIVAALKAKDAELS 183
Cdd:PRK11414  185 YRLLLAALKAKDKEGC 200
PRK03837 PRK03837
transcriptional regulator NanR; Provisional
4-193 8.01e-10

transcriptional regulator NanR; Provisional


Pssm-ID: 235166 [Multi-domain]  Cd Length: 241  Bit Score: 56.95  E-value: 8.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   4 EIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLV---------YLVPNRGVFIKRVTR--------- 64
Cdd:PRK03837   21 RLEQMIRSGEFGPGDQLpSERELMAFFGVGRPAVREALQALKRKGLVqishgerarVSRPSADTIIGQLSGmakdflsqs 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  65 DDAIEVYD-LRTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAekGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAF 143
Cdd:PRK03837  101 PDGLAHLKqARLFFESSLARYAAEHATDEQIALLRKALERNSQSL--GDNAAFIRSDMEFHRVIAEIPGNPIFMAIHEAL 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2635381164 144 VKEFHLFRVHGLVQRGALLESNAEHREIVAALKAKDAELSYRASFGHVSR 193
Cdd:PRK03837  179 LDWLIEARPEVVILHGHENVTLQEHIAIVDAIRAHDPDEADRALQSHLNR 228
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
3-69 1.35e-09

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 56.02  E-value: 1.35e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2635381164   3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIE 69
Cdd:COG2188    12 DALRERIESGELPPGDRLpSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLS 79
PRK10225 PRK10225
Uxu operon transcriptional regulator;
5-199 1.69e-09

Uxu operon transcriptional regulator;


Pssm-ID: 182318 [Multi-domain]  Cd Length: 257  Bit Score: 56.18  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   5 IERMILSGELAPGQRLN-EKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDL---------- 73
Cdd:PRK10225   18 IRDLIIKTPYNPGERLPpEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAGIYVLDSSGSHNTDSPDAnvcndagpfe 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  74 ----RTGLTALSASLLAPMLTQE------MAGQLE--RYVDDMQDAAEKGDfahfdplnLEFHDYIVRSTGNSRLIRLYR 141
Cdd:PRK10225   98 llqaRQLLESNIAEFAALQATREdivkmrQALQLEerELASSAPGSSESGD--------MQFHLAIAEATHNSMLVELFR 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2635381164 142 AFVK---------EFHLFRVHGLVQRGALlesnAEHREIVAALKAKDAELSYRASFGHVSRGKERML 199
Cdd:PRK10225  170 QSWQwrennpmwiQLHSHLDDSLYRKEWL----GDHKQILAALIKKDARAAKLAMWQHLENVKQRLL 232
pdhR PRK09464
pyruvate dehydrogenase complex transcriptional repressor PdhR;
4-199 2.35e-06

pyruvate dehydrogenase complex transcriptional repressor PdhR;


Pssm-ID: 181879 [Multi-domain]  Cd Length: 254  Bit Score: 46.94  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   4 EIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIK------------RVTRDDAIEV 70
Cdd:PRK09464   18 QLEFLILEGTLRPGEKLpPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGGGTFVQsslwqsfsdplvELLSDHPESQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  71 YDL---RTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKGDFAHFDPLNLEFHDYIVRSTGNSRLIRLYRAFVKEF 147
Cdd:PRK09464   98 FDLletRHALEGIAAYYAALRGTDEDFERIRECHHAIELAQQSGDLDAEANAVMQYQIAVTEAAHNVVLLHLLRCMEPML 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2635381164 148 H---LFRVHGLVQRGALLESNAEHR-EIVAALKAKDAELSYRASFGHVSRGKERML 199
Cdd:PRK09464  178 EqnvRQNFELLYRRREMLPKVSSHRaRIFEAIVAGKPEKAREASHRHLAFIEEILL 233
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
3-69 1.28e-05

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 45.20  E-value: 1.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2635381164   3 REIERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIE 69
Cdd:COG1167    19 DALREAILSGRLPPGDRLpSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPA 86
PRK11534 PRK11534
DNA-binding transcriptional regulator CsiR; Provisional
3-181 1.52e-05

DNA-binding transcriptional regulator CsiR; Provisional


Pssm-ID: 183181 [Multi-domain]  Cd Length: 224  Bit Score: 44.50  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   3 REIERMILSGELAPGQRLNEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIEVYDLRTGLTAL-- 80
Cdd:PRK11534   14 RWLKNDIIRGNFQPDEKLRMSLLTSRYALGVGPLREALSQLVAERLVTVVNQKGYRVASMSEQELLDIFDARANMEAMlv 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  81 -----------SASLLApmlTQEMAGQLERyVDDMQDAAEKGDFAHfdplnLEFHDYIVRSTGNSRLI----RLYRAFVK 145
Cdd:PRK11534   94 slaiarggdewEADVLA---KAHLLSKLEA-CDASEKMLDEWDLRH-----QAFHTAIVAGCGSHYLLqmreRLFDLAAR 164
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2635381164 146 EFHLFRVHGLVQRGALLESNAEHREIVAALKAKDAE 181
Cdd:PRK11534  165 YRFIWLRRTVLSVEMLEDKHDQHQTLTAAILARDTA 200
PRK09990 PRK09990
DNA-binding transcriptional regulator GlcC; Provisional
5-137 2.03e-05

DNA-binding transcriptional regulator GlcC; Provisional


Pssm-ID: 182186 [Multi-domain]  Cd Length: 251  Bit Score: 44.37  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   5 IERMILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLVYLVPNRGVFIKRVTRDDAIE------------VY 71
Cdd:PRK09990   16 IERLIVDGVLKVGQALpSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRGSFVARLNRVQDASplmhlfssqprtLY 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2635381164  72 DL---RTGLTALSASLLAPMLTQEMAGQLERYVDDMQDAAEKG---DFAHFDPLNLEFHDYIVRSTGNSRLI 137
Cdd:PRK09990   96 DLlevRALLEGESARLAALRGTQADFVLITRRYEEMLAAHENNkeiDPIEHARLDHAFHLAICEASHNPVLV 167
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
8-192 2.51e-05

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 43.99  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164   8 MILSGELAPGQRL-NEKAVADKLAVSRGPVREACRALTELGLvyLVPNR--GVF----------------IKRVTRDDAI 68
Cdd:PRK10421   14 LIEEKNLEAGMKLpAERQLAMQLGVSRNSLREALAKLVSEGV--LLSRRggGTFirwrhetwseqnivqpLKTLMADDPD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164  69 EVYDL---RTGLTALSASLLAPMLTQEMAGQLERYVDDMQ----DAAEKGDfahfdplnLEFHDYIVRSTGNSRLIRLYR 141
Cdd:PRK10421   92 YSFDIleaRHAIEASTAWHAAMRATPGDKEKIQLCFEATLsedpDLASQAD--------VRFHLAIAEASHNVVLLQTMR 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2635381164 142 AFvkeFHLfrVHGLVQRG---------ALLESNAEHREIVAALKAKDAELSYRASFGHVS 192
Cdd:PRK10421  164 GF---FDV--LQSSVKQSrqrmylvppVFSQLTEQHQAVMDAILAGDAEGARKAMMAHLS 218
 
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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