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Conserved domains on  [gi|488290829|ref|WP_002362037|]
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MULTISPECIES: transcriptional regulator YeiL [Enterococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10402 super family cl28241
DNA-binding transcriptional activator YeiL; Provisional
 31-220 1.07e-48

DNA-binding transcriptional activator YeiL; Provisional


The actual alignment was detected with superfamily member PRK10402:

Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 159.12  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  31 IIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVPLA 110
Cdd:PRK10402  33 LFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKAVQAIEECWCLALPMK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 111 YAETVLKNKVLFMQQLSHYLGKKMLQRVDHFTTNQTYELSYRLAELLLVAAnHEDVYKEKHTEIAEYLGVSYRHLIYTFK 190
Cdd:PRK10402 113 DCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFILLTQ-EGDLYHEKHTQAAEYLGVSYRHLLYVLA 191

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488290829 191 QFRERGFIQKQGTAYHI-NRLALHSFVQKMK 220
Cdd:PRK10402 192 QFIQDGYLKKSKRGYLIkNRKQLSGLALELK 222
 
Name Accession Description Interval E-value
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 31-220 1.07e-48

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 159.12  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  31 IIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVPLA 110
Cdd:PRK10402  33 LFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKAVQAIEECWCLALPMK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 111 YAETVLKNKVLFMQQLSHYLGKKMLQRVDHFTTNQTYELSYRLAELLLVAAnHEDVYKEKHTEIAEYLGVSYRHLIYTFK 190
Cdd:PRK10402 113 DCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFILLTQ-EGDLYHEKHTQAAEYLGVSYRHLLYVLA 191

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488290829 191 QFRERGFIQKQGTAYHI-NRLALHSFVQKMK 220
Cdd:PRK10402 192 QFIQDGYLKKSKRGYLIkNRKQLSGLALELK 222
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 26-216 4.40e-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: 105.45  E-value: 4.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  26 LKHSFIIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCL 105
Cdd:COG0664   13 LAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 106 AVPLAYAETVLKNKVLFMQQLSHYLGKKMLQRVDHFTTNQTYELSYRLAELLLVAANHEDVYKE---KHTEIAEYLGVSY 182
Cdd:COG0664   93 RIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGRIDlplTQEEIASYLGLTR 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488290829 183 RHLIYTFKQFRERGFIQKQGTAYHI-NRLALHSFV 216
Cdd:COG0664  173 ETVSRILKKLEKEGLIELERGRITIlDREALERLA 207
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 34-118 1.82e-16

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: 71.49  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829   34 FENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVPLAYAE 113
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFL 83


                  ....*
gi 488290829  114 TVLKN 118
Cdd:pfam00027  84 ELLER 88
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 38-108 1.59e-09

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: 53.87  E-value: 1.59e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488290829  38 EFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVP 108
Cdd:cd00038   26 EVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLP 96
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 38-126 6.48e-07

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: 46.63  E-value: 6.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829    38 EFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETI--TKDVIALGETCCLAVPLAYAETV 115
Cdd:smart00100  26 EVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRaaSAAAVALELATLLRIDFRDFLQL 105

                           90
                   ....*....|.
gi 488290829   116 LKNKVLFMQQL 126
Cdd:smart00100 106 LPELPQLLLEL 116
 
Name Accession Description Interval E-value
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 31-220 1.07e-48

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 159.12  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  31 IIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVPLA 110
Cdd:PRK10402  33 LFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKAVQAIEECWCLALPMK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 111 YAETVLKNKVLFMQQLSHYLGKKMLQRVDHFTTNQTYELSYRLAELLLVAAnHEDVYKEKHTEIAEYLGVSYRHLIYTFK 190
Cdd:PRK10402 113 DCRPLLLNDALFLRKLCKFLSHKNYRNIVSLTQNQSFPLENRLAAFILLTQ-EGDLYHEKHTQAAEYLGVSYRHLLYVLA 191

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488290829 191 QFRERGFIQKQGTAYHI-NRLALHSFVQKMK 220
Cdd:PRK10402 192 QFIQDGYLKKSKRGYLIkNRKQLSGLALELK 222
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 26-216 4.40e-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: 105.45  E-value: 4.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  26 LKHSFIIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCL 105
Cdd:COG0664   13 LAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 106 AVPLAYAETVLKNKVLFMQQLSHYLGKKMLQRVDHFTTNQTYELSYRLAELLLVAANHEDVYKE---KHTEIAEYLGVSY 182
Cdd:COG0664   93 RIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGRIDlplTQEEIASYLGLTR 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488290829 183 RHLIYTFKQFRERGFIQKQGTAYHI-NRLALHSFV 216
Cdd:COG0664  173 ETVSRILKKLEKEGLIELERGRITIlDREALERLA 207
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 34-118 1.82e-16

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: 71.49  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829   34 FENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVPLAYAE 113
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFL 83


                  ....*
gi 488290829  114 TVLKN 118
Cdd:pfam00027  84 ELLER 88
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 38-108 1.59e-09

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: 53.87  E-value: 1.59e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488290829  38 EFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETITKDVIALGETCCLAVP 108
Cdd:cd00038   26 EVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLP 96
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
26-202 4.12e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 48.82  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829  26 LKHSFIIDFENQEFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVqAETITKDVIALGETCCL 105
Cdd:PRK11753  17 LSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLF-EEGQERSAWVRAKTACE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829 106 AVPLAYAetvlKNKVLFMQ--QLSHYLGKKMLQRVDHfTTNQTYELSY-----RLAELLL------VAANHEDVYKEKHT 172
Cdd:PRK11753  96 VAEISYK----KFRQLIQVnpDILMALSAQMARRLQN-TSRKVGDLAFldvtgRIAQTLLdlakqpDAMTHPDGMQIKIT 170

                        170       180       190
                 ....*....|....*....|....*....|..
gi 488290829 173 --EIAEYLGVSYRHLIYTFKQFRERGFIQKQG 202
Cdd:PRK11753 171 rqEIGRIVGCSREMVGRVLKMLEDQGLISAHG 202
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 38-126 6.48e-07

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: 46.63  E-value: 6.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488290829    38 EFIHHQAEPLNYLFYLIKGKAKILKTERNGRQSIVQFLTTGDLIGDLTLVQAETI--TKDVIALGETCCLAVPLAYAETV 115
Cdd:smart00100  26 EVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRaaSAAAVALELATLLRIDFRDFLQL 105

                           90
                   ....*....|.
gi 488290829   116 LKNKVLFMQQL 126
Cdd:smart00100 106 LPELPQLLLEL 116
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 152-202 1.76e-05

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: 41.29  E-value: 1.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488290829  152 RLAELLLVAANHEDVYKEK----HTEIAEYLGVSYRHLIYTFKQFRERGFIQKQG 202
Cdd:pfam13545   2 RLARFLLELAARDGGGRIDlpltQEDLADLLGTTRETVSRVLSELRREGLIERGR 56
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 152-209 4.11e-04

helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.


Pssm-ID: 238044 [Multi-domain]  Cd Length: 67  Bit Score: 37.65  E-value: 4.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488290829 152 RLAELLLVAANHEDVYKE-----KHTEIAEYLGVSYRHLIYTFKQFRERGFIQKQGT-AYHINR 209
Cdd:cd00092    4 RLASFLLNLSLRYGAGDLvqlplTRQEIADYLGLTRETVSRTLKELEEEGLISRRGRgKYRVNP 67
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
171-208 4.16e-03

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 34.34  E-value: 4.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 488290829   171 HTEIAEYLGVSYRHLIYTFKQFRERGFIQKQGTAYHIN 208
Cdd:smart00419  11 RQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVIL 48
 
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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