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Conserved domains on  [gi|1315370158|ref|NP_001346030|]
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cAMP-dependent protein kinase type I-beta regulatory subunit isoform b [Mus musculus]

Protein Classification

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

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP)

CATH:  2.60.120.10
Gene Ontology:  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 ...
 131-246 5.76e-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: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 131 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 210
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1315370158 211 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 246
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 13-122 5.21e-29

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: 105.87  E-value: 5.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  13 LFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 87
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1315370158  88 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 122
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 131-246 5.76e-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: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 131 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 210
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1315370158 211 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 246
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 13-122 5.21e-29

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: 105.87  E-value: 5.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  13 LFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 87
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1315370158  88 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 122
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 131-249 8.90e-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: 100.17  E-value: 8.90e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  131 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 208
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1315370158  209 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 249
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 13-127 1.68e-25

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: 97.09  E-value: 1.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158   13 LFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 87
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1315370158   88 AATVKAKTdLKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 127
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 149-235 1.09e-20

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: 83.43  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 149 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 228
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 1315370158 229 PRFERVL 235
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 132-235 1.39e-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: 78.49  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 132 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 211
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 1315370158 212 AATVVARGPLKCVKLDRPRFERVL 235
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 37-112 2.29e-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: 71.87  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  37 GETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:pfam00027   7 GEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLELL 86


                  .
gi 1315370158 112 M 112
Cdd:pfam00027  87 E 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 14-111 1.68e-14

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: 70.02  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  14 FSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRA 88
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSP 80

                          90       100
                  ....*....|....*....|...
gi 1315370158  89 ATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELL 103
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 124-226 3.32e-11

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.43  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 124 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 203
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 1315370158 204 aLLLNRPRAATVVARGPLKCVKL 226
Cdd:PLN02868   85 -GLSGSVHSADVVAVSELTCLVL 106
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 150-217 3.09e-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: 3.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1315370158 150 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 217
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 12-111 4.90e-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: 40.65  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  12 VLFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-P 86
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 1315370158  87 RAATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
39-119 5.64e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  39 TVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 108
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 1315370158 109 ---RILM--GSTLRKR 119
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 ...
 131-246 5.76e-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: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 131 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 210
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1315370158 211 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 246
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 13-122 5.21e-29

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: 105.87  E-value: 5.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  13 LFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 87
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1315370158  88 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 122
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 131-249 8.90e-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: 100.17  E-value: 8.90e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  131 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 208
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1315370158  209 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 249
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 13-127 1.68e-25

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: 97.09  E-value: 1.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158   13 LFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 87
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1315370158   88 AATVKAKTdLKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 127
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 149-235 1.09e-20

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: 83.43  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 149 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 228
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 1315370158 229 PRFERVL 235
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 132-235 1.39e-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: 78.49  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 132 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 211
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 1315370158 212 AATVVARGPLKCVKLDRPRFERVL 235
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 37-112 2.29e-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: 71.87  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  37 GETVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:pfam00027   7 GEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLELL 86


                  .
gi 1315370158 112 M 112
Cdd:pfam00027  87 E 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 14-111 1.68e-14

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: 70.02  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  14 FSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRA 88
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSP 80

                          90       100
                  ....*....|....*....|...
gi 1315370158  89 ATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELL 103
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 124-226 3.32e-11

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.43  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 124 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 203
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 1315370158 204 aLLLNRPRAATVVARGPLKCVKL 226
Cdd:PLN02868   85 -GLSGSVHSADVVAVSELTCLVL 106
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 150-217 3.09e-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: 3.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1315370158 150 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 217
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
158-242 6.88e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 42.66  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 158 IVVQGEPGDDFYIITEGTASVLQRRSPNEEYVeVGRLGPSDYFGEIALLL-NRPRAATVVARGPLKCVKLDRPRFERVLG 236
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMI-LSYLNQGDFIGELGLFEeGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....*.
gi 1315370158 237 PCSEIL 242
Cdd:PRK11753  110 VNPDIL 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-214 1.32e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1315370158 156 EKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVevGRLGPSDYFGEIALLLNRPRAAT 214
Cdd:PLN03192  406 EDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVV--GTLGCGDIFGEVGALCCRPQSFT 462
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 37-228 1.89e-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: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  37 GETVIQQGNEGDNFYVIDQGEVDVYVNGEW---------VTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSY 107
Cdd:TIGR03896  16 GTTLIEEGKAADFLFILLDGTFTVTTPQPEdnpltrafeLARLSRGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVGEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158 108 RRILMGSTLRKRKMYEEFLSKVS-----------------------ILESLEKWERLTVA---DALEPVQFEDGEKIVVQ 161
Cdd:TIGR03896  96 AAKLQSDVGFAAHFYRAIAIKLAlqiqnqnhqlhrrngadseplrkVLFIFGELHESDVAwmmASGTPQKLPAGTILIHE 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1315370158 162 GEPGDDFYIITEGTASVLQrrSPNEEYVEVGRLGPSDYFGEIALL-LNRPRAATVVARGPLKCVKLDR 228
Cdd:TIGR03896 176 GGTVDALYILLYGEASLSI--SPDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLLAIDK 241
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 12-111 4.90e-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: 40.65  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  12 VLFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-P 86
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 1315370158  87 RAATVKAKTDLKLWGIDRDSYRRIL 111
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
39-119 5.64e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315370158  39 TVIQQGNEGDNFYVIDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 108
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 1315370158 109 ---RILM--GSTLRKR 119
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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