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Conserved domains on  [gi|112293405|gb|ABI14854|]
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CNGC5-like protein, partial [Medicago sativa subsp. glomerata]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10034975)

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP) where binding of the effector leads to conformational changes; may be involved in regulating transcription, be present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK), or be part of vertebrate cyclic nucleotide-gated ion-channels.

CATH:  2.60.120.10
Gene Ontology:  GO:0030552|GO:0030551
SCOP:  4000272

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
3-122 2.32e-16

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: 69.28  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   3 LFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLESVTTDGGrSGFFNRTYLKEAEFCGEELLTwald 82
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDED-GREQIVGFLGPGDLFGELALL---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 112293405  83 prsgsNLPTSTRTVKALTEVETFALTADELKFVASQFRRL 122
Cdd:cd00038   76 -----GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
3-122 2.32e-16

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: 69.28  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   3 LFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLESVTTDGGrSGFFNRTYLKEAEFCGEELLTwald 82
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDED-GREQIVGFLGPGDLFGELALL---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 112293405  83 prsgsNLPTSTRTVKALTEVETFALTADELKFVASQFRRL 122
Cdd:cd00038   76 -----GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
3-122 3.47e-09

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: 50.86  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405     3 LFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLEsVTTDGGRSGFFNRTYLKEAEFCGEE-LLTWAL 81
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVE-VYKVLEDGEEQIVGTLGPGDFFGELaLLTNSR 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 112293405    82 DPRSgsnlptstRTVKALTEVETFALTADELKFVASQFRRL 122
Cdd:smart00100  80 RAAS--------AAAVALELATLLRIDFRDFLQLLPELPQL 112
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
4-113 4.21e-08

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: 49.21  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   4 FESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLESVTTD-GGRSgfFNRTYLKEAEFCGEELLtwaLD 82
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGRE--QILGFLGPGDFFGELSL---LG 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 112293405  83 PRsgsnlpTSTRTVKALTEVETFALTADELK 113
Cdd:COG0664   76 GE------PSPATAEALEDSELLRIPREDLE 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
24-112 1.36e-07

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: 45.68  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   24 FTENTYIVREGDPVDEMLFIIRGRLESVTTDG-GRSGFFNRtyLKEAEFCGE-ELLTwaLDPRSGsnlptstrTVKALTE 101
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdGREQILAV--LGPGDFFGElALLG--GEPRSA--------TVVALTD 71
                          90
                  ....*....|.
gi 112293405  102 VETFALTADEL 112
Cdd:pfam00027  72 SELLVIPREDF 82
PLN02868 PLN02868
acyl-CoA thioesterase family protein
1-49 1.38e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 37.01  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 112293405   1 VPLFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLE 49
Cdd:PLN02868  13 VPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAE 61
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
3-122 2.32e-16

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: 69.28  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   3 LFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLESVTTDGGrSGFFNRTYLKEAEFCGEELLTwald 82
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDED-GREQIVGFLGPGDLFGELALL---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 112293405  83 prsgsNLPTSTRTVKALTEVETFALTADELKFVASQFRRL 122
Cdd:cd00038   76 -----GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
3-122 3.47e-09

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: 50.86  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405     3 LFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLEsVTTDGGRSGFFNRTYLKEAEFCGEE-LLTWAL 81
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVE-VYKVLEDGEEQIVGTLGPGDFFGELaLLTNSR 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 112293405    82 DPRSgsnlptstRTVKALTEVETFALTADELKFVASQFRRL 122
Cdd:smart00100  80 RAAS--------AAAVALELATLLRIDFRDFLQLLPELPQL 112
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
4-113 4.21e-08

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: 49.21  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   4 FESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLESVTTD-GGRSgfFNRTYLKEAEFCGEELLtwaLD 82
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGRE--QILGFLGPGDFFGELSL---LG 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 112293405  83 PRsgsnlpTSTRTVKALTEVETFALTADELK 113
Cdd:COG0664   76 GE------PSPATAEALEDSELLRIPREDLE 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
24-112 1.36e-07

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: 45.68  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293405   24 FTENTYIVREGDPVDEMLFIIRGRLESVTTDG-GRSGFFNRtyLKEAEFCGE-ELLTwaLDPRSGsnlptstrTVKALTE 101
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdGREQILAV--LGPGDFFGElALLG--GEPRSA--------TVVALTD 71
                          90
                  ....*....|.
gi 112293405  102 VETFALTADEL 112
Cdd:pfam00027  72 SELLVIPREDF 82
PLN02868 PLN02868
acyl-CoA thioesterase family protein
1-49 1.38e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 37.01  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 112293405   1 VPLFESMDERLLDAICERLKPCLFTENTYIVREGDPVDEMLFIIRGRLE 49
Cdd:PLN02868  13 VPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAE 61
 
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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