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Conserved domains on  [gi|446581233|ref|WP_000658579|]
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MULTISPECIES: transcriptional regulator YeiL [Enterobacteriaceae]

Protein Classification

transcriptional regulator YeiL( domain architecture ID 11484696)

transcriptional regulator YeiL is involved in mid-term, stationary-phase viability under nitrogen starvation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 1-226 4.38e-154

DNA-binding transcriptional activator YeiL; Provisional


:

Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 426.84  E-value: 4.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233   1 MKEIHNNDLKQQLMSESAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAP 80
Cdd:PRK10402   1 MKESKNSEEISHYMSESAFKDCFSFDVSADTELFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  81 CFIGEIELIDKDHEPRAVQAIEECWCLALPMKHYRPRLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFIL 160
Cdd:PRK10402  81 CFIGEIELIDKDHETKAVQAIEECWCLALPMKDCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581233 161 LSQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLALEMDPENK 226
Cdd:PRK10402 161 LTQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIQDGYLKKSKRGYLIKNRKQLSGLALELKPENK 226
 
Name Accession Description Interval E-value
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 1-226 4.38e-154

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 426.84  E-value: 4.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233   1 MKEIHNNDLKQQLMSESAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAP 80
Cdd:PRK10402   1 MKESKNSEEISHYMSESAFKDCFSFDVSADTELFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  81 CFIGEIELIDKDHEPRAVQAIEECWCLALPMKHYRPRLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFIL 160
Cdd:PRK10402  81 CFIGEIELIDKDHETKAVQAIEECWCLALPMKDCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581233 161 LSQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLALEMDPENK 226
Cdd:PRK10402 161 LTQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIQDGYLKKSKRGYLIKNRKQLSGLALELKPENK 226
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 24-218 2.77e-28

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 106.22  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  24 LTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEE 103
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALED 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233 104 CWCLALPMKHYRPRLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFIL-LSQEGDLYHE---KHTQAAEYL 179
Cdd:COG0664   89 SELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLeLADRLDGRIDlplTQEEIASYL 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446581233 180 GVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLA 218
Cdd:COG0664  169 GLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 17-128 5.47e-18

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 76.60  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  17 SAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPR 96
Cdd:cd00038    3 SGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSA 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446581233  97 AVQAIEECWCLALPMKHYRPRLLNDTLFLRKL 128
Cdd:cd00038   83 TVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 17-132 3.38e-15

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 69.35  E-value: 3.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233    17 SAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPR 96
Cdd:smart00100   3 KNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAA 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 446581233    97 --AVQAIEECWCLALPMKHYRPRLLNDTLFLRKLCVTL 132
Cdd:smart00100  83 saAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 33-115 3.64e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 65.71  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233   33 LFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEECWCLALPMK 112
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ...
gi 446581233  113 HYR 115
Cdd:pfam00027  81 DFL 83
 
Name Accession Description Interval E-value
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 1-226 4.38e-154

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 426.84  E-value: 4.38e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233   1 MKEIHNNDLKQQLMSESAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAP 80
Cdd:PRK10402   1 MKESKNSEEISHYMSESAFKDCFSFDVSADTELFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  81 CFIGEIELIDKDHEPRAVQAIEECWCLALPMKHYRPRLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFIL 160
Cdd:PRK10402  81 CFIGEIELIDKDHETKAVQAIEECWCLALPMKDCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581233 161 LSQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLALEMDPENK 226
Cdd:PRK10402 161 LTQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIQDGYLKKSKRGYLIKNRKQLSGLALELKPENK 226
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 24-218 2.77e-28

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 106.22  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  24 LTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEE 103
Cdd:COG0664    9 LEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALED 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233 104 CWCLALPMKHYRPRLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFIL-LSQEGDLYHE---KHTQAAEYL 179
Cdd:COG0664   89 SELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLeLADRLDGRIDlplTQEEIASYL 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446581233 180 GVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLA 218
Cdd:COG0664  169 GLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 17-128 5.47e-18

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 76.60  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233  17 SAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPR 96
Cdd:cd00038    3 SGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSA 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446581233  97 AVQAIEECWCLALPMKHYRPRLLNDTLFLRKL 128
Cdd:cd00038   83 TVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 17-132 3.38e-15

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 69.35  E-value: 3.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233    17 SAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPR 96
Cdd:smart00100   3 KNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAA 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 446581233    97 --AVQAIEECWCLALPMKHYRPRLLNDTLFLRKLCVTL 132
Cdd:smart00100  83 saAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 33-115 3.64e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 65.71  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581233   33 LFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEECWCLALPMK 112
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ...
gi 446581233  113 HYR 115
Cdd:pfam00027  81 DFL 83
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 154-214 3.57e-03

Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.


Pssm-ID: 463917 [Multi-domain]  Cd Length: 68  Bit Score: 35.13  E-value: 3.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581233  154 RLAAFIL-LSQEGDLYHEK----HTQAAEYLGVSYRHLLYVLAQFIHDGLLikSKKGYLIKNRKQL 214
Cdd:pfam13545   2 RLARFLLeLAARDGGGRIDlpltQEDLADLLGTTRETVSRVLSELRREGLI--ERGRITILDPEAL 65
 
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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