NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1381930513|ref|NP_001349606|]
View 

cAMP-dependent protein kinase type I-alpha regulatory subunit [Mus musculus]

Protein Classification

cyclic nucleotide-binding domain-containing protein; cyclic nucleotide-gated ion channel( domain architecture ID 10186668)

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.| cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 255-370 7.62e-31

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: 7.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 255 ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRP 334
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1381930513 335 RAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNI 370
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DD_RIalpha_PKA cd12101
dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent ...
 14-63 2.03e-30

dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent protein kinase; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha is the key regulatory subunit responsible for maintaining cAMP control of the catalytic subunit. RIalpha function is required for normal development as its deletion is embryonically lethal due to failed cardiac morphogenesis. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


:

Pssm-ID: 438522  Cd Length: 50  Bit Score: 110.42  E-value: 2.03e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1381930513  14 SLRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEAR 63
Cdd:cd12101     1 SLRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK 50
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 9.92e-30

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: 110.88  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 137 LFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSV-----GEGGSFGELALIYGTPR 211
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQivgflGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1381930513 212 AATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMY 246
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 ...
 255-370 7.62e-31

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: 7.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 255 ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRP 334
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1381930513 335 RAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNI 370
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DD_RIalpha_PKA cd12101
dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent ...
 14-63 2.03e-30

dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent protein kinase; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha is the key regulatory subunit responsible for maintaining cAMP control of the catalytic subunit. RIalpha function is required for normal development as its deletion is embryonically lethal due to failed cardiac morphogenesis. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 438522  Cd Length: 50  Bit Score: 110.42  E-value: 2.03e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1381930513  14 SLRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEAR 63
Cdd:cd12101     1 SLRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK 50
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 9.92e-30

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: 110.88  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 137 LFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSV-----GEGGSFGELALIYGTPR 211
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQivgflGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1381930513 212 AATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMY 246
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-251 2.31e-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: 104.79  E-value: 2.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513  137 LFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNE-----WATSVGEGGSFGELALIYGTPR 211
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1381930513  212 AATVKAKTnVKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 251
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 255-373 4.97e-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: 103.63  E-value: 4.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513  255 ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMN-- 332
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY-KVLEDGEEQIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1381930513  333 RPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQY 373
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 273-359 9.29e-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: 85.74  E-value: 9.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 273 PVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDR 352
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 1381930513 353 PRFERVL 359
Cdd:pfam00027  80 EDFLELL 86
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-236 3.82e-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: 75.72  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 155 PVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNE-----WATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRD 229
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*..
gi 1381930513 230 SYRRILM 236
Cdd:pfam00027  81 DFLELLE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 256-359 8.61e-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: 78.10  E-value: 8.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 256 LESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRPR 335
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 1381930513 336 AATVVARGPLKCVKLDRPRFERVL 359
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-235 2.34e-16

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: 76.95  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 138 FSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSV-----GEGGSFGELALIYGTPRA 212
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQilgflGPGDFFGELSLLGGEPSP 80

                          90       100
                  ....*....|....*....|...
gi 1381930513 213 ATVKAKTNVKLWGIDRDSYRRIL 235
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELL 103
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 25-62 7.50e-12

RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit portion of type II PKA R-subunit. Contains dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).


Pssm-ID: 197697  Cd Length: 38  Bit Score: 59.27  E-value: 7.50e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1381930513   25 HNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEA 62
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
25-61 8.63e-12

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 59.25  E-value: 8.63e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1381930513  25 HNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEE 61
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 248-350 1.66e-09

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 58.96  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 248 EFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqrRSENEEFVEVGRLGPSDYFGEi 327
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS--GPAEEESRPEFLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 1381930513 328 ALLMNRpRAATVVARGPLKCVKL 350
Cdd:PLN02868   85 GLSGSV-HSADVVAVSELTCLVL 106
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 136-235 2.95e-06

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: 48.74  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 136 VLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVN-NEWATSVG---EGGSFGELALIYGT-P 210
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISpDGPGREVGssrRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 1381930513 211 RAATVKAKTNVKLWGIDRDSYRRIL 235
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 274-341 3.37e-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: 45.27  E-value: 3.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1381930513 274 VQFE--DGQKIVVQGEPGDEFFIILEGTAAVLQRRSEN---EEFVEVGRLGPSDYFGEIALLMNRPRAATVVA 341
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDnplTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
163-243 3.07e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.42  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 163 TVIQQGDEGDNFYVIDQGEMDVYVNNEWA-----TSVGEGGSFGELAL-IYGTPRAATVKAKTNVKLWGIDRDSYR---- 232
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEEGkemilSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 1381930513 233 ---RILM--GSTLRKR 243
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 ...
 255-370 7.62e-31

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: 7.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 255 ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRP 334
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1381930513 335 RAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNI 370
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DD_RIalpha_PKA cd12101
dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent ...
 14-63 2.03e-30

dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent protein kinase; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha is the key regulatory subunit responsible for maintaining cAMP control of the catalytic subunit. RIalpha function is required for normal development as its deletion is embryonically lethal due to failed cardiac morphogenesis. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 438522  Cd Length: 50  Bit Score: 110.42  E-value: 2.03e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1381930513  14 SLRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEAR 63
Cdd:cd12101     1 SLRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK 50
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 9.92e-30

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: 110.88  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 137 LFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSV-----GEGGSFGELALIYGTPR 211
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQivgflGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1381930513 212 AATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMY 246
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-251 2.31e-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: 104.79  E-value: 2.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513  137 LFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNE-----WATSVGEGGSFGELALIYGTPR 211
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1381930513  212 AATVKAKTnVKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 251
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 255-373 4.97e-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: 103.63  E-value: 4.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513  255 ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMN-- 332
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY-KVLEDGEEQIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1381930513  333 RPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQY 373
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
DD_RI_PKA cd12097
dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein ...
 15-63 8.06e-26

dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein kinase; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha function is required for normal development as its deletion is embryonically lethal. RIbeta is expressed highly in the brain and is associated with hippocampal function. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 438518  Cd Length: 49  Bit Score: 97.99  E-value: 8.06e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1381930513  15 LRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEAR 63
Cdd:cd12097     1 LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR 49
DD_RIbeta_PKA cd12102
dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent ...
 11-64 1.52e-22

dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent protein kinase; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIbeta is expressed highly in the brain and is associated with hippocampal function. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 438523  Cd Length: 54  Bit Score: 89.62  E-value: 1.52e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1381930513  11 EERSLRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEARQ 64
Cdd:cd12102     1 EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ 54
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 273-359 9.29e-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: 85.74  E-value: 9.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 273 PVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDR 352
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 1381930513 353 PRFERVL 359
Cdd:pfam00027  80 EDFLELL 86
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-236 3.82e-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: 75.72  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 155 PVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNE-----WATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRD 229
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*..
gi 1381930513 230 SYRRILM 236
Cdd:pfam00027  81 DFLELLE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 256-359 8.61e-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: 78.10  E-value: 8.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 256 LESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqRRSENEEFVEVGRLGPSDYFGEIALLMNRPR 335
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                          90       100
                  ....*....|....*....|....
gi 1381930513 336 AATVVARGPLKCVKLDRPRFERVL 359
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELL 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-235 2.34e-16

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: 76.95  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 138 FSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSV-----GEGGSFGELALIYGTPRA 212
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQilgflGPGDFFGELSLLGGEPSP 80

                          90       100
                  ....*....|....*....|...
gi 1381930513 213 ATVKAKTNVKLWGIDRDSYRRIL 235
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELL 103
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 25-62 7.50e-12

RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit portion of type II PKA R-subunit. Contains dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).


Pssm-ID: 197697  Cd Length: 38  Bit Score: 59.27  E-value: 7.50e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1381930513   25 HNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEA 62
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
25-61 8.63e-12

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 59.25  E-value: 8.63e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1381930513  25 HNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEE 61
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 248-350 1.66e-09

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 58.96  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 248 EFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLqrRSENEEFVEVGRLGPSDYFGEi 327
Cdd:PLN02868    8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS--GPAEEESRPEFLLKRYDYFGY- 84

                          90       100
                  ....*....|....*....|...
gi 1381930513 328 ALLMNRpRAATVVARGPLKCVKL 350
Cdd:PLN02868   85 GLSGSV-HSADVVAVSELTCLVL 106
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 17-57 2.40e-07

dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438530  Cd Length: 43  Bit Score: 46.64  E-value: 2.40e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1381930513  17 ECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERL 57
Cdd:cd22961     3 DAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 136-235 2.95e-06

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: 48.74  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 136 VLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVN-NEWATSVG---EGGSFGELALIYGT-P 210
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISpDGPGREVGssrRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 1381930513 211 RAATVKAKTNVKLWGIDRDSYRRIL 235
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 16-57 7.25e-06

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 10 (EFCAB10) and similar proteins; The subfamily includes uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438545  Cd Length: 47  Bit Score: 42.86  E-value: 7.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1381930513  16 RECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERL 57
Cdd:cd22976     2 EEAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKL 43
DD_C11orf49 cd22959
dimerization/docking (D/D) domain found in UPF0705 protein C11orf49 and similar proteins; ...
 21-59 8.00e-06

dimerization/docking (D/D) domain found in UPF0705 protein C11orf49 and similar proteins; UPF0705 protein C11orf49 is an uncharacterized protein which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438528  Cd Length: 53  Bit Score: 42.92  E-value: 8.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1381930513  21 YVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEK 59
Cdd:cd22959     3 YLERHGVLVYLEDAVTQLLENRPENPAKFLAEYFRSVLK 41
DD_AtENO3-like cd22962
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ...
 21-57 1.78e-05

dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. The subfamily includes Arabidopsis thaliana ENO3, also called ENOC, 2-phospho-D-glycerate hydro-lyase 3, or 2-phosphoglycerate dehydratase 3. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438531  Cd Length: 45  Bit Score: 41.41  E-value: 1.78e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1381930513  21 YVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERL 57
Cdd:cd22962     6 YLEKHKLEEKLEEAVNAVVKEKPEDPFGFLAQLLRKR 42
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 21-56 1.88e-05

dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and similar proteins; AK (EC 2.7.4.3), also called ATP-AMP transphosphorylase, ATP:AMP phosphotransferase, or adenylate monophosphate kinase, catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Members of this subfamily contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438550  Cd Length: 44  Bit Score: 41.25  E-value: 1.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1381930513  21 YVQKHNIQALLkDSIVQ-LCTTRPERPMAFLREYFER 56
Cdd:cd22981     8 YLKEKNIPQLF-EFLLRhLLLDKPENPLEYLHDLLER 43
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
282-366 2.32e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 44.97  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 282 IVVQGEPGDEFFIILEGTAAVLQRRSENEEFVeVGRLGPSDYFGEIALLM-NRPRAATVVARGPLKCVKLDRPRFERVLG 360
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMI-LSYLNQGDFIGELGLFEeGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                  ....*.
gi 1381930513 361 PCSDIL 366
Cdd:PRK11753  110 VNPDIL 115
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 274-341 3.37e-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: 45.27  E-value: 3.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1381930513 274 VQFE--DGQKIVVQGEPGDEFFIILEGTAAVLQRRSEN---EEFVEVGRLGPSDYFGEIALLMNRPRAATVVA 341
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDnplTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
 29-57 4.58e-05

dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory subunit (PRKAR) and the DPY30/SDC1-like family; This hierarchy includes the dimerization/docking (D/D) domains of type I and type II cAMP-dependent protein kinase (PKA) regulatory (R) subunits, DPY30 from animals and its homologs, SDC1 from yeasts, and similar domains. PKA is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of R subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal D/D domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1 (suppressor of CDC25 protein 1) is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DPY30/SDC1 contains a C-terminal helical bundle domain that directly interacts with Ash2L (in human)/Bre2 (in yeast) COMPASS through the DPY30-binding motif (DBM). The DPY30/SDC1 helical bundle domain, also called D/D domain, is formed of two alpha-helices that may be analogous to the D/D domain found in regulatory subunit of PKA.


Pssm-ID: 438526  Cd Length: 29  Bit Score: 39.79  E-value: 4.58e-05
                          10        20
                  ....*....|....*....|....*....
gi 1381930513  29 ALLKDSIVQLCTTRPERPMAFLREYFERL 57
Cdd:cd22957     1 ELLQDAVAKLLEERPEDPVEFLAEYFEKA 29
DD_TPGS1 cd22960
dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) ...
 21-58 5.16e-05

dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) and similar proteins; TPGS1 is part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. It is required for the development of the spermatid flagellum. TPGS1 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438529  Cd Length: 39  Bit Score: 39.88  E-value: 5.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1381930513  21 YVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLE 58
Cdd:cd22960     2 FLERTGVTSLLRDALLKVLENRPEDPIAFLAEYFESLA 39
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 160-352 1.68e-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: 42.96  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 160 AGETVIQQGDEGDNFYVIDQGEMDVYVNNE------WATSVGE---GGSFGELALIYGTPRAATVKAKTNVKLWGIDRDS 230
Cdd:TIGR03896  15 AGTTLIEEGKAADFLFILLDGTFTVTTPQPednpltRAFELARlsrGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVGE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 231 YRRILMGSTLRKRKMYEEFLSKVS-----------------------ILESLDKWERLTVA---DALEPVQFEDGQKIVV 284
Cdd:TIGR03896  95 LAAKLQSDVGFAAHFYRAIAIKLAlqiqnqnhqlhrrngadseplrkVLFIFGELHESDVAwmmASGTPQKLPAGTILIH 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1381930513 285 QGEPGDEFFIILEGTAAVLQrrSENEEFVEVGRLGPSDYFGEIALL-MNRPRAATVVARGPLKCVKLDR 352
Cdd:TIGR03896 175 EGGTVDALYILLYGEASLSI--SPDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLLAIDK 241
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 19-56 2.31e-03

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar proteins; AK8 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 8, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK8 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438548  Cd Length: 45  Bit Score: 35.52  E-value: 2.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1381930513  19 ELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFER 56
Cdd:cd22979     7 AAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 280-338 2.74e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 2.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1381930513 280 QKIVVQGEPGDEFFIILEGTAAVLQRRSENEEFVevGRLGPSDYFGEIALLMNRPRAAT 338
Cdd:PLN03192  406 EDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVV--GTLGCGDIFGEVGALCCRPQSFT 462
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
163-243 3.07e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.42  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381930513 163 TVIQQGDEGDNFYVIDQGEMDVYVNNEWA-----TSVGEGGSFGELAL-IYGTPRAATVKAKTNVKLWGIDRDSYR---- 232
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEEGkemilSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                          90
                  ....*....|....*.
gi 1381930513 233 ---RILM--GSTLRKR 243
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH