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Conserved domains on  [gi|987005265|gb|AMD50856|]
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cAMP-binding protein [Listeria monocytogenes]

Protein Classification

Crp/Fnr family transcriptional regulator( domain architecture ID 11429533)

Crp/Fnr family transcriptional regulator containing a DNA-binding Crp-like helix-turn-helix (HTH) domain, may bind cyclic nucleotides

CATH:  2.60.120.10|1.10.10.10
Gene Ontology:  GO:0003677|GO:0030552
PubMed:  11407111|14638413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 14-215 5.77e-17

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: 76.18  E-value: 5.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  14 DYSSKISFKKGEIIHsyrDYEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRAL 93
Cdd:COG0664   14 AHLELRTLKKGEVLF---REGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP----ATAEAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  94 ENGTVLFIDREFLLNYLYANPQFFHLILDEVIVRYLFTSKNYKNINQAPIV-KVTRILVEIIEllhlhQTEGSIELPVyv 172
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEeRLARFLLELAD-----RLDGRIDLPL-- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 987005265 173 TQTFLADYCRSSRARVTEVLEELRESGLL-LSKKPITISSHENL 215
Cdd:COG0664  160 TQEEIASYLGLTRETVSRILKKLEKEGLIeLERGRITILDREAL 203
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 14-215 5.77e-17

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: 76.18  E-value: 5.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  14 DYSSKISFKKGEIIHsyrDYEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRAL 93
Cdd:COG0664   14 AHLELRTLKKGEVLF---REGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP----ATAEAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  94 ENGTVLFIDREFLLNYLYANPQFFHLILDEVIVRYLFTSKNYKNINQAPIV-KVTRILVEIIEllhlhQTEGSIELPVyv 172
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEeRLARFLLELAD-----RLDGRIDLPL-- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 987005265 173 TQTFLADYCRSSRARVTEVLEELRESGLL-LSKKPITISSHENL 215
Cdd:COG0664  160 TQEEIASYLGLTRETVSRILKKLEKEGLIeLERGRITILDREAL 203
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 18-110 7.27e-08

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: 48.76  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265   18 KISFKKGEIIhsYRDyEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRALENGT 97
Cdd:pfam00027   1 LRSYKAGEVI--FRE-GDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRS----ATVVALTDSE 73

                          90
                  ....*....|...
gi 987005265   98 VLFIDREFLLNYL 110
Cdd:pfam00027  74 LLVIPREDFLELL 86
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 13-116 4.49e-07

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: 47.32  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  13 SDYSSKISFKKGEIIhsYRdYEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRA 92
Cdd:cd00038   14 ADALEERRFPAGEVI--IR-QGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRS----ATVRA 86

                         90       100
                 ....*....|....*....|....
gi 987005265  93 LENGTVLFIDREFLLNYLYANPQF 116
Cdd:cd00038   87 LTDSELLVLPRSDFRRLLQEYPEL 110
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 14-215 5.77e-17

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: 76.18  E-value: 5.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  14 DYSSKISFKKGEIIHsyrDYEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRAL 93
Cdd:COG0664   14 AHLELRTLKKGEVLF---REGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP----ATAEAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  94 ENGTVLFIDREFLLNYLYANPQFFHLILDEVIVRYLFTSKNYKNINQAPIV-KVTRILVEIIEllhlhQTEGSIELPVyv 172
Cdd:COG0664   87 EDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEeRLARFLLELAD-----RLDGRIDLPL-- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 987005265 173 TQTFLADYCRSSRARVTEVLEELRESGLL-LSKKPITISSHENL 215
Cdd:COG0664  160 TQEEIASYLGLTRETVSRILKKLEKEGLIeLERGRITILDREAL 203
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 18-110 7.27e-08

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: 48.76  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265   18 KISFKKGEIIhsYRDyEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRALENGT 97
Cdd:pfam00027   1 LRSYKAGEVI--FRE-GDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRS----ATVVALTDSE 73

                          90
                  ....*....|...
gi 987005265   98 VLFIDREFLLNYL 110
Cdd:pfam00027  74 LLVIPREDFLELL 86
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 13-116 4.49e-07

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: 47.32  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987005265  13 SDYSSKISFKKGEIIhsYRdYEEKAPQIGAILEGTAVLEGPTNEGRWMINALIGQHALFGMESLLETKTAPelteYRVRA 92
Cdd:cd00038   14 ADALEERRFPAGEVI--IR-QGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRS----ATVRA 86

                         90       100
                 ....*....|....*....|....
gi 987005265  93 LENGTVLFIDREFLLNYLYANPQF 116
Cdd:cd00038   87 LTDSELLVLPRSDFRRLLQEYPEL 110
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 156-209 3.82e-06

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: 43.21  E-value: 3.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 987005265  156 LLHLHQTEGSIELPVYVTQTFLADYCRSSRARVTEVLEELRESGlLLSKKPITI 209
Cdd:pfam13545   7 LLELAARDGGGRIDLPLTQEDLADLLGTTRETVSRVLSELRREG-LIERGRITI 59
 
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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