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Conserved domains on  [gi|5822234|pdb|1QC7|A]
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Chain A, PROTEIN (FLIG)

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FliG super family cl34298
Flagellar motor switch protein FliG [Cell motility];
1-99 2.84e-56

Flagellar motor switch protein FliG [Cell motility];


The actual alignment was detected with superfamily member COG1536:

Pssm-ID: 441145 [Multi-domain]  Cd Length: 337  Bit Score: 176.87  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A        1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:COG1536 239 MFVFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKIFSNMSKRAAEMLREDLEAMGPVRLSDVEEAQKEIVAIA 318

                        90
                ....*....|....*....
1QC7_A       81 RRLEEAGEIVIARGGGEEL 99
Cdd:COG1536 319 RRLAEEGEIVLGRGGGDEY 337
 
Name Accession Description Interval E-value
FliG COG1536
Flagellar motor switch protein FliG [Cell motility];
1-99 2.84e-56

Flagellar motor switch protein FliG [Cell motility];


Pssm-ID: 441145 [Multi-domain]  Cd Length: 337  Bit Score: 176.87  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A        1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:COG1536 239 MFVFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKIFSNMSKRAAEMLREDLEAMGPVRLSDVEEAQKEIVAIA 318

                        90
                ....*....|....*....
1QC7_A       81 RRLEEAGEIVIARGGGEEL 99
Cdd:COG1536 319 RRLAEEGEIVLGRGGGDEY 337
fliG PRK05686
flagellar motor switch protein G; Validated
 1-100 1.25e-51

flagellar motor switch protein G; Validated


Pssm-ID: 235561 [Multi-domain]  Cd Length: 339  Bit Score: 164.97  E-value: 1.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A         1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:PRK05686 241 MFVFEDLVDLDDRSIQRLLREVDNDVLALALKGASEELREKFLSNMSKRAAEMLREDLEALGPVRLSDVEEAQKKIVQIA 320

                         90       100
                 ....*....|....*....|
1QC7_A        81 RRLEEAGEIVIarGGGEELI 100
Cdd:PRK05686 321 RRLAEAGEIVL--GGGDDEI 338
FliG_C pfam01706
FliG C-terminal domain; FliG is a component of the flageller rotor, present in about 25 copies ...
 1-91 3.65e-45

FliG C-terminal domain; FliG is a component of the flageller rotor, present in about 25 copies per flagellum. This domain functions specifically in motor rotation.


Pssm-ID: 460301 [Multi-domain]  Cd Length: 108  Bit Score: 141.07  E-value: 3.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A          1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:pfam01706  18 MFTFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKILSNMSKRAAEMLREELEALGPVRLSDVEEAQKEIVAIA 97

                          90
                  ....*....|.
1QC7_A         81 RRLEEAGEIVI 91
Cdd:pfam01706  98 RRLEEEGEIVL 108
fliG TIGR00207
flagellar motor switch protein FliG; The fliG protein along with fliM and fliN interact to ...
 1-100 6.20e-43

flagellar motor switch protein FliG; The fliG protein along with fliM and fliN interact to form the switch complex of the bacterial flagellar motor located at the base of the basal body. This complex interacts with chemotaxis proteins (eg CHEY). In addition the complex interacts with other components of the motor that determine the direction of flagellar rotation. The model contains putative members of the fliG family at scores of less than 100 from Agrobacterium radiobacter and Sinorhizobium meliloti as well as fliG-like genes from treponema pallidum and Borrelia burgdorferi. That is why the suggested cutoff is set at 20 but was set at 100 to construct the family. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 272961 [Multi-domain]  Cd Length: 338  Bit Score: 142.65  E-value: 6.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A          1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:TIGR00207 238 MFVFEDIVDLDDRSIQRVLREVDSEDLLLALKGAEQPLREKFLNNMSQRAAEILKEDMEFLGPVRLKDVEEAQKKIVSIV 317

                          90       100
                  ....*....|....*....|
1QC7_A         81 RRLEEAGEIVIARGGGEELI 100
Cdd:TIGR00207 318 RKLEETGEIVIGRGGEEDVI 337
 
Name Accession Description Interval E-value
FliG COG1536
Flagellar motor switch protein FliG [Cell motility];
1-99 2.84e-56

Flagellar motor switch protein FliG [Cell motility];


Pssm-ID: 441145 [Multi-domain]  Cd Length: 337  Bit Score: 176.87  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A        1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:COG1536 239 MFVFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKIFSNMSKRAAEMLREDLEAMGPVRLSDVEEAQKEIVAIA 318

                        90
                ....*....|....*....
1QC7_A       81 RRLEEAGEIVIARGGGEEL 99
Cdd:COG1536 319 RRLAEEGEIVLGRGGGDEY 337
fliG PRK05686
flagellar motor switch protein G; Validated
 1-100 1.25e-51

flagellar motor switch protein G; Validated


Pssm-ID: 235561 [Multi-domain]  Cd Length: 339  Bit Score: 164.97  E-value: 1.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A         1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:PRK05686 241 MFVFEDLVDLDDRSIQRLLREVDNDVLALALKGASEELREKFLSNMSKRAAEMLREDLEALGPVRLSDVEEAQKKIVQIA 320

                         90       100
                 ....*....|....*....|
1QC7_A        81 RRLEEAGEIVIarGGGEELI 100
Cdd:PRK05686 321 RRLAEAGEIVL--GGGDDEI 338
FliG_C pfam01706
FliG C-terminal domain; FliG is a component of the flageller rotor, present in about 25 copies ...
 1-91 3.65e-45

FliG C-terminal domain; FliG is a component of the flageller rotor, present in about 25 copies per flagellum. This domain functions specifically in motor rotation.


Pssm-ID: 460301 [Multi-domain]  Cd Length: 108  Bit Score: 141.07  E-value: 3.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A          1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:pfam01706  18 MFTFEDLVRLDDRSIQRLLREVDNDDLALALKGASEELREKILSNMSKRAAEMLREELEALGPVRLSDVEEAQKEIVAIA 97

                          90
                  ....*....|.
1QC7_A         81 RRLEEAGEIVI 91
Cdd:pfam01706  98 RRLEEEGEIVL 108
fliG TIGR00207
flagellar motor switch protein FliG; The fliG protein along with fliM and fliN interact to ...
 1-100 6.20e-43

flagellar motor switch protein FliG; The fliG protein along with fliM and fliN interact to form the switch complex of the bacterial flagellar motor located at the base of the basal body. This complex interacts with chemotaxis proteins (eg CHEY). In addition the complex interacts with other components of the motor that determine the direction of flagellar rotation. The model contains putative members of the fliG family at scores of less than 100 from Agrobacterium radiobacter and Sinorhizobium meliloti as well as fliG-like genes from treponema pallidum and Borrelia burgdorferi. That is why the suggested cutoff is set at 20 but was set at 100 to construct the family. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 272961 [Multi-domain]  Cd Length: 338  Bit Score: 142.65  E-value: 6.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A          1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:TIGR00207 238 MFVFEDIVDLDDRSIQRVLREVDSEDLLLALKGAEQPLREKFLNNMSQRAAEILKEDMEFLGPVRLKDVEEAQKKIVSIV 317

                          90       100
                  ....*....|....*....|
1QC7_A         81 RRLEEAGEIVIARGGGEELI 100
Cdd:TIGR00207 318 RKLEETGEIVIGRGGEEDVI 337
fliG PRK07194
flagellar motor switch protein G; Reviewed
 1-89 3.21e-17

flagellar motor switch protein G; Reviewed


Pssm-ID: 235958 [Multi-domain]  Cd Length: 334  Bit Score: 74.26  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QC7_A         1 MFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINII 80
Cdd:PRK07194 235 MYDFFILSRQSEETLQRLMDEVPMELWAVALKGTEPALRQAILRVMPKRQAQALEAQIERLGPVPLSRVEQARKEIMALV 314


                 ....*....
1QC7_A        81 RRLEEAGEI 89
Cdd:PRK07194 315 RELAEAGEI 323
 
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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