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Conserved domains on  [gi|2217367850|ref|XP_047276566|]
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cAMP-dependent protein kinase type I-beta regulatory subunit isoform X3 [Homo sapiens]

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
PubMed:  6280140|12087135|17601606|11734894
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 ...
 103-218 3.05e-32

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: 113.57  E-value: 3.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 103 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 182
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217367850 183 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 218
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-94 7.65e-24

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: 91.62  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGID 75
Cdd:cd00038    17 LEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLP 96

                          90
                  ....*....|....*....
gi 2217367850  76 RDSYRRILMGSTLRKRKMY 94
Cdd:cd00038    97 RSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 103-218 3.05e-32

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: 113.57  E-value: 3.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 103 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 182
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217367850 183 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 218
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 103-221 3.76e-27

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: 100.55  E-value: 3.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  103 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 180
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217367850  181 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 221
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-94 7.65e-24

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: 91.62  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGID 75
Cdd:cd00038    17 LEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLP 96

                          90
                  ....*....|....*....
gi 2217367850  76 RDSYRRILMGSTLRKRKMY 94
Cdd:cd00038    97 RSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 121-207 9.04e-21

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: 83.04  E-value: 9.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 121 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 200
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 2217367850 201 PRFERVL 207
Cdd:pfam00027  80 EDFLELL 86
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 1-99 9.98e-21

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: 83.99  E-value: 9.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850    1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTdLKLWGID 75
Cdd:smart00100  17 LEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRRAASAAAVA-LELATLL 95

                           90       100
                   ....*....|....*....|....
gi 2217367850   76 RDSYRRILMGSTLRKRKMYEEFLS 99
Cdd:smart00100  96 RIDFRDFLQLLPELPQLLLELLLE 119
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 104-207 7.38e-18

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: 78.49  E-value: 7.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 104 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 183
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 2217367850 184 AATVVARGPLKCVKLDRPRFERVL 207
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 8-84 5.58e-17

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: 73.03  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   8 AGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRI 82
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 2217367850  83 LM 84
Cdd:pfam00027  86 LE 87
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 96-198 2.09e-11

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.43  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  96 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 175
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 2217367850 176 aLLLNRPRAATVVARGPLKCVKL 198
Cdd:PLN02868   85 -GLSGSVHSADVVAVSELTCLVL 106
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 1-83 2.91e-11

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: 60.77  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGID 75
Cdd:COG0664    16 LELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIP 95


                  ....*...
gi 2217367850  76 RDSYRRIL 83
Cdd:COG0664    96 REDLEELL 103
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 122-189 2.42e-05

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 44.50  E-value: 2.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217367850 122 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 189
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 3-83 1.62e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 41.80  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   3 PVTHIAGETVIQQGNEGDNFYVVDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-PRAATVKAKTDLKLWGIDRD 77
Cdd:TIGR03896 163 PQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlPGTATVKAIENSVLLAIDKQ 242


                  ....*.
gi 2217367850  78 SYRRIL 83
Cdd:TIGR03896 243 QLAAKL 248
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
11-91 1.18e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  11 TVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 80
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 2217367850  81 ---RILM--GSTLRKR 91
Cdd:PRK11753  110 vnpDILMalSAQMARR 125
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 103-218 3.05e-32

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: 113.57  E-value: 3.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 103 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 182
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217367850 183 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 218
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 103-221 3.76e-27

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: 100.55  E-value: 3.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  103 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 180
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217367850  181 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 221
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-94 7.65e-24

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: 91.62  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGID 75
Cdd:cd00038    17 LEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLP 96

                          90
                  ....*....|....*....
gi 2217367850  76 RDSYRRILMGSTLRKRKMY 94
Cdd:cd00038    97 RSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 121-207 9.04e-21

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: 83.04  E-value: 9.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 121 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 200
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 2217367850 201 PRFERVL 207
Cdd:pfam00027  80 EDFLELL 86
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 1-99 9.98e-21

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: 83.99  E-value: 9.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850    1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTdLKLWGID 75
Cdd:smart00100  17 LEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRRAASAAAVA-LELATLL 95

                           90       100
                   ....*....|....*....|....
gi 2217367850   76 RDSYRRILMGSTLRKRKMYEEFLS 99
Cdd:smart00100  96 RIDFRDFLQLLPELPQLLLELLLE 119
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 104-207 7.38e-18

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: 78.49  E-value: 7.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 104 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 183
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 2217367850 184 AATVVARGPLKCVKLDRPRFERVL 207
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 8-84 5.58e-17

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: 73.03  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   8 AGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRI 82
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 2217367850  83 LM 84
Cdd:pfam00027  86 LE 87
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 96-198 2.09e-11

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.43  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  96 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 175
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 2217367850 176 aLLLNRPRAATVVARGPLKCVKL 198
Cdd:PLN02868   85 -GLSGSVHSADVVAVSELTCLVL 106
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 1-83 2.91e-11

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: 60.77  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   1 MFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGID 75
Cdd:COG0664    16 LELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIP 95


                  ....*...
gi 2217367850  76 RDSYRRIL 83
Cdd:COG0664    96 REDLEELL 103
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 122-189 2.42e-05

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 44.50  E-value: 2.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217367850 122 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 189
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 8-200 4.40e-05

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 43.73  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   8 AGETVIQQGNEGDNFYVVDQGEVDVYVNGEW---------VTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDS 78
Cdd:TIGR03896  15 AGTTLIEEGKAADFLFILLDGTFTVTTPQPEdnpltrafeLARLSRGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVGE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  79 YRRILMGSTLRKRKMYEEFLSKVS-----------------------ILESLEKWERLTVA---DALEPVQFEDGEKIVV 132
Cdd:TIGR03896  95 LAAKLQSDVGFAAHFYRAIAIKLAlqiqnqnhqlhrrngadseplrkVLFIFGELHESDVAwmmASGTPQKLPAGTILIH 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217367850 133 QGEPGDDFYIITEGTASVLQrrSPNEEYVEVGRLGPSDYFGEIALL-LNRPRAATVVARGPLKCVKLDR 200
Cdd:TIGR03896 175 EGGTVDALYILLYGEASLSI--SPDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLLAIDK 241
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
130-214 5.65e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 42.66  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850 130 IVVQGEPGDDFYIITEGTASVLQRRSPNEEYVeVGRLGPSDYFGEIALLL-NRPRAATVVARGPLKCVKLDRPRFERVLG 208
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMI-LSYLNQGDFIGELGLFEeGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....*.
gi 2217367850 209 PCSEIL 214
Cdd:PRK11753  110 VNPDIL 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 128-186 8.62e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 8.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217367850 128 EKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVevGRLGPSDYFGEIALLLNRPRAAT 186
Cdd:PLN03192  406 EDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVV--GTLGCGDIFGEVGALCCRPQSFT 462
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 3-83 1.62e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 41.80  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850   3 PVTHIAGETVIQQGNEGDNFYVVDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-PRAATVKAKTDLKLWGIDRD 77
Cdd:TIGR03896 163 PQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlPGTATVKAIENSVLLAIDKQ 242


                  ....*.
gi 2217367850  78 SYRRIL 83
Cdd:TIGR03896 243 QLAAKL 248
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
11-91 1.18e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217367850  11 TVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 80
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 2217367850  81 ---RILM--GSTLRKR 91
Cdd:PRK11753  110 vnpDILMalSAQMARR 125
 
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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