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Conserved domains on  [gi|16128729|ref|NP_415282|]
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DNA-binding transcriptional dual regulator ModE [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

molybdenum-dependent transcriptional regulator( domain architecture ID 11484868)

molybdenum-dependent DNA-binding transcriptional regulator represses the modABCD operon and activates the moaABCD and napFDAGHBC operons

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10676 PRK10676
DNA-binding transcriptional regulator ModE; Provisional
 1-262 4.03e-172

DNA-binding transcriptional regulator ModE; Provisional


:

Pssm-ID: 182640 [Multi-domain]  Cd Length: 263  Bit Score: 474.91  E-value: 4.03e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729    1 MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80
Cdd:PRK10676   1 MQAEILLTLKLQQRLFADPRRISLLKQIALTGSISQGAKLAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   81 YGQRLIQLYDLLAQIQQKAFDVLsDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKV 160
Cdd:PRK10676  81 YGERLIQLYDLLAQIQQKAFDVL-DDDALPLDSLLAAISRFSLQTSARNQWFGTITARDHQQVQQHVDVLLADGKTRLKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729  161 AITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEAT- 239
Cdd:PRK10676 160 AITAQSAERLGLDEGKEVLVLIKAPWVGITQDPAVAQAADNQLPGTISHIERGAEQSEVLMALPDGQTLCATVPNNEAAr 239

                        250       260
                 ....*....|....*....|....
gi 16128729  240 -SLQQGQNVTAYFNADSVIIATLC 262
Cdd:PRK10676 240 lSLQQGDAVTAYFNADRVIIATLC 263
 
Name Accession Description Interval E-value
PRK10676 PRK10676
DNA-binding transcriptional regulator ModE; Provisional
 1-262 4.03e-172

DNA-binding transcriptional regulator ModE; Provisional


Pssm-ID: 182640 [Multi-domain]  Cd Length: 263  Bit Score: 474.91  E-value: 4.03e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729    1 MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80
Cdd:PRK10676   1 MQAEILLTLKLQQRLFADPRRISLLKQIALTGSISQGAKLAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   81 YGQRLIQLYDLLAQIQQKAFDVLsDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKV 160
Cdd:PRK10676  81 YGERLIQLYDLLAQIQQKAFDVL-DDDALPLDSLLAAISRFSLQTSARNQWFGTITARDHQQVQQHVDVLLADGKTRLKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729  161 AITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEAT- 239
Cdd:PRK10676 160 AITAQSAERLGLDEGKEVLVLIKAPWVGITQDPAVAQAADNQLPGTISHIERGAEQSEVLMALPDGQTLCATVPNNEAAr 239

                        250       260
                 ....*....|....*....|....
gi 16128729  240 -SLQQGQNVTAYFNADSVIIATLC 262
Cdd:PRK10676 240 lSLQQGDAVTAYFNADRVIIATLC 263
ModE_repress TIGR00637
ModE molybdate transport repressor domain; ModE is a molybdate-activated repressor of the ...
 16-113 4.26e-43

ModE molybdate transport repressor domain; ModE is a molybdate-activated repressor of the molybdate transport operon in E. coli. It consists of the domain represented by this model and two tandem copies of mop-like domain, where Mop proteins are a family of 68-residue molybdenum-pterin binding proteins of Clostridium pasteurianum. This model also represents the full length of a pair of archaeal proteins that lack Mop-like domains. PSI-BLAST analysis shows similarity to helix-turn-helix regulatory proteins. [Regulatory functions, Other]


Pssm-ID: 273188 [Multi-domain]  Cd Length: 99  Bit Score: 141.81  E-value: 4.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729    16 FADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQI 95
Cdd:TIGR00637   1 FADPRRVALLKAIARMGSISQAAKDAGISYKSAWDYIRAMNNLSGEPLVERATGGKGGGGAVLTEYGQRLIQLYDLLERI 80

                          90
                  ....*....|....*....
gi 16128729    96 QQKAFDVLSDDD-ALPLNS 113
Cdd:TIGR00637  81 LEKAFSVLEDEVvVKPLKA 99
MopI COG3585
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
124-262 6.52e-42

Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];


Pssm-ID: 442804 [Multi-domain]  Cd Length: 141  Bit Score: 140.21  E-value: 6.52e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729 124 QTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQL 203
Cdd:COG3585   1 MTSSRNNQFGGVVSIIAGGVVNEVVLLLLGGGTIIAAITTASSAELLGLVGGKEVAALKKASVVILATDDAMKLSARNQL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128729 204 PGIISHIERGAEQCEVLMALPDGQTLCATVPvNEAT---SLQQGQNVTAYFNADSVIIATLC 262
Cdd:COG3585  81 KGTVTRIERGAVNSEVVLDLGGGTTLTAVIT-NESVeelGLKEGDEVTALFKASSVILAVDA 141
TOBE pfam03459
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 199-256 1.55e-10

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.


Pssm-ID: 427310 [Multi-domain]  Cd Length: 60  Bit Score: 55.36  E-value: 1.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   199 ADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQ--QGQNVTAYFNADSV 256
Cdd:pfam03459   1 ARNQLPGTVTVIEPLGSEVEVRVDLGGGLTLTARITRDSAEELGlaPGDEVWALIKATKV 60
 
Name Accession Description Interval E-value
PRK10676 PRK10676
DNA-binding transcriptional regulator ModE; Provisional
 1-262 4.03e-172

DNA-binding transcriptional regulator ModE; Provisional


Pssm-ID: 182640 [Multi-domain]  Cd Length: 263  Bit Score: 474.91  E-value: 4.03e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729    1 MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80
Cdd:PRK10676   1 MQAEILLTLKLQQRLFADPRRISLLKQIALTGSISQGAKLAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   81 YGQRLIQLYDLLAQIQQKAFDVLsDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKV 160
Cdd:PRK10676  81 YGERLIQLYDLLAQIQQKAFDVL-DDDALPLDSLLAAISRFSLQTSARNQWFGTITARDHQQVQQHVDVLLADGKTRLKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729  161 AITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEAT- 239
Cdd:PRK10676 160 AITAQSAERLGLDEGKEVLVLIKAPWVGITQDPAVAQAADNQLPGTISHIERGAEQSEVLMALPDGQTLCATVPNNEAAr 239

                        250       260
                 ....*....|....*....|....
gi 16128729  240 -SLQQGQNVTAYFNADSVIIATLC 262
Cdd:PRK10676 240 lSLQQGDAVTAYFNADRVIIATLC 263
ModE_repress TIGR00637
ModE molybdate transport repressor domain; ModE is a molybdate-activated repressor of the ...
 16-113 4.26e-43

ModE molybdate transport repressor domain; ModE is a molybdate-activated repressor of the molybdate transport operon in E. coli. It consists of the domain represented by this model and two tandem copies of mop-like domain, where Mop proteins are a family of 68-residue molybdenum-pterin binding proteins of Clostridium pasteurianum. This model also represents the full length of a pair of archaeal proteins that lack Mop-like domains. PSI-BLAST analysis shows similarity to helix-turn-helix regulatory proteins. [Regulatory functions, Other]


Pssm-ID: 273188 [Multi-domain]  Cd Length: 99  Bit Score: 141.81  E-value: 4.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729    16 FADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQI 95
Cdd:TIGR00637   1 FADPRRVALLKAIARMGSISQAAKDAGISYKSAWDYIRAMNNLSGEPLVERATGGKGGGGAVLTEYGQRLIQLYDLLERI 80

                          90
                  ....*....|....*....
gi 16128729    96 QQKAFDVLSDDD-ALPLNS 113
Cdd:TIGR00637  81 LEKAFSVLEDEVvVKPLKA 99
MopI COG3585
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
124-262 6.52e-42

Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];


Pssm-ID: 442804 [Multi-domain]  Cd Length: 141  Bit Score: 140.21  E-value: 6.52e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729 124 QTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQL 203
Cdd:COG3585   1 MTSSRNNQFGGVVSIIAGGVVNEVVLLLLGGGTIIAAITTASSAELLGLVGGKEVAALKKASVVILATDDAMKLSARNQL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128729 204 PGIISHIERGAEQCEVLMALPDGQTLCATVPvNEAT---SLQQGQNVTAYFNADSVIIATLC 262
Cdd:COG3585  81 KGTVTRIERGAVNSEVVLDLGGGTTLTAVIT-NESVeelGLKEGDEVTALFKASSVILAVDA 141
ModE COG2005
DNA-binding transcriptional regulator ModE (molybdenum-dependent) [Transcription];
16-117 4.28e-31

DNA-binding transcriptional regulator ModE (molybdenum-dependent) [Transcription];


Pssm-ID: 441608 [Multi-domain]  Cd Length: 118  Bit Score: 111.45  E-value: 4.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729  16 FADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQI 95
Cdd:COG2005  18 FLGPGRIELLEAIDETGSISAAAKAMGMSYKRAWDLIDAMNNLLGEPLVERQTGGKGGGGARLTPEGRRLLALYRRLEAE 97

                        90       100
                ....*....|....*....|..
gi 16128729  96 QQKAFDVLSDDdalpLNSLLAA 117
Cdd:COG2005  98 AQRALAALFEE----LFALLRS 115
Mop TIGR00638
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ...
 123-192 5.87e-28

molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins. [Transport and binding proteins, Anions]


Pssm-ID: 273189 [Multi-domain]  Cd Length: 69  Bit Score: 102.05  E-value: 5.87e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   123 LQTSARNQWFGTITARDHDDVQQHVDVLLAdGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQD 192
Cdd:TIGR00638   1 LQTSARNQLKGKVVAIEDGDVNAEVDLLLG-GGTKLTAVITLESVAELGLKPGKEVYAVIKAPWVILAVD 69
TOBE pfam03459
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 199-256 1.55e-10

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.


Pssm-ID: 427310 [Multi-domain]  Cd Length: 60  Bit Score: 55.36  E-value: 1.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128729   199 ADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQ--QGQNVTAYFNADSV 256
Cdd:pfam03459   1 ARNQLPGTVTVIEPLGSEVEVRVDLGGGLTLTARITRDSAEELGlaPGDEVWALIKATKV 60
MopI COG3585
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
123-184 1.46e-08

Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];


Pssm-ID: 442804 [Multi-domain]  Cd Length: 141  Bit Score: 52.39  E-value: 1.46e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128729 123 LQTSARNQWFGTITARDHDDVQQHVDVLLADGKTrLKVAITAQSGARLGLDEGKEVLILLKA 184
Cdd:COG3585  72 MKLSARNQLKGTVTRIERGAVNSEVVLDLGGGTT-LTAVITNESVEELGLKEGDEVTALFKA 132
TOBE pfam03459
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 127-187 1.56e-08

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.


Pssm-ID: 427310 [Multi-domain]  Cd Length: 60  Bit Score: 49.97  E-value: 1.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128729   127 ARNQWFGTITARDHDDVQQHVDVLLADGKTrLKVAITAQSGARLGLDEGKEVLILLKAPWV 187
Cdd:pfam03459   1 ARNQLPGTVTVIEPLGSEVEVRVDLGGGLT-LTARITRDSAEELGLAPGDEVWALIKATKV 60
Mop TIGR00638
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ...
 199-260 8.36e-04

molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins. [Transport and binding proteins, Anions]


Pssm-ID: 273189 [Multi-domain]  Cd Length: 69  Bit Score: 36.95  E-value: 8.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128729   199 ADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQ--QGQNVTAYFNADSVIIAT 260
Cdd:TIGR00638   5 ARNQLKGKVVAIEDGDVNAEVDLLLGGGTKLTAVITLESVAELGlkPGKEVYAVIKAPWVILAV 68
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 199-258 7.63e-03

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 34.52  E-value: 7.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128729   199 ADNQLPGIISHIE-RGAEQcEVLMALPDGQTLCATVPVNEATSLQQGQNVTAYFNADSVII 258
Cdd:pfam08402  13 AANGLSGTVTDVEyLGDHT-RYHVELAGGEELVVRVPNAHARPPAPGDRVGLGWDPEDAHV 72
 
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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