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Conserved domains on  [gi|47132585|ref|NP_002727|]
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cAMP-dependent protein kinase type II-beta regulatory subunit [Homo sapiens]

Protein Classification

DD_RIIbeta_PKA and CAP_ED domain-containing protein( domain architecture ID 10186682)

DD_RIIbeta_PKA and CAP_ED domain-containing protein

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 ...
 154-267 2.00e-26

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: 102.40  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 154 LFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVK-CDGVGRCVGNYDNRGSFGELALMYNTPR 232
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdEDGREQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47132585 233 AATITATSPGALWGLDRVTFRRIIVKNNAKKRKMY 267
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 276-396 2.38e-26

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: 102.40  E-value: 2.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 276 FLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEengaveIARCSRGQYFGELAL 355
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQI------VGFLGPGDLFGELAL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132585 356 VTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNI 396
Cdd:cd00038  75 LGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DD_RIIbeta_PKA cd12104
dimerization/docking (D/D) domain of the Type II beta Regulatory subunit of cAMP-dependent ...
 3-45 5.40e-23

dimerization/docking (D/D) domain of the Type II 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIbeta plays an important role in adipocytes and neuronal tissues. Mice deficient with RIIbeta have small fat cells, and are resistant to obesity, diet-induced diabetes, and alcohol-induced motor defects. 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: 438525  Cd Length: 43  Bit Score: 90.73  E-value: 5.40e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 47132585   3 IEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENER 45
Cdd:cd12104   1 IEIPEGLTELLQGFTVEVLRNQPGDLLEFALQYFTRLKQAQSK 43
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 154-267 2.00e-26

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: 102.40  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 154 LFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVK-CDGVGRCVGNYDNRGSFGELALMYNTPR 232
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdEDGREQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47132585 233 AATITATSPGALWGLDRVTFRRIIVKNNAKKRKMY 267
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 276-396 2.38e-26

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: 102.40  E-value: 2.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 276 FLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEengaveIARCSRGQYFGELAL 355
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQI------VGFLGPGDLFGELAL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132585 356 VTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNI 396
Cdd:cd00038  75 LGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 154-272 6.86e-24

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: 95.55  E-value: 6.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585    154 LFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVK-CDGVGRCVGNYDNRGSFGELALMYNTPR 232
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVlEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 47132585    233 AATITATSPGaLWGLDRVTFRRIIVKNNAKKRKMYESFIE 272
Cdd:smart00100  81 AASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 276-399 1.62e-23

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: 94.78  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585    276 FLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITmkrkgkSEVEENGAVEIARCSRGQYFGELAL 355
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY------KVLEDGEEQIVGTLGPGDFFGELAL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 47132585    356 VTNKPRAASAHAIGT--VKCLAMDVQAFERLLGPCMEIMKRNIATY 399
Cdd:smart00100  75 LTNSRRAASAAAVALelATLLRIDFRDFLQLLPELPQLLLELLLEL 120
DD_RIIbeta_PKA cd12104
dimerization/docking (D/D) domain of the Type II beta Regulatory subunit of cAMP-dependent ...
 3-45 5.40e-23

dimerization/docking (D/D) domain of the Type II 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIbeta plays an important role in adipocytes and neuronal tissues. Mice deficient with RIIbeta have small fat cells, and are resistant to obesity, diet-induced diabetes, and alcohol-induced motor defects. 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: 438525  Cd Length: 43  Bit Score: 90.73  E-value: 5.40e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 47132585   3 IEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENER 45
Cdd:cd12104   1 IEIPEGLTELLQGFTVEVLRNQPGDLLEFALQYFTRLKQAQSK 43
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 295-385 3.66e-18

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: 78.81  E-value: 3.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   295 KVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEengaveIARCSRGQYFGELALVTNKPRAASAHAIGTVKCL 374
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI------LAVLGPGDFFGELALLGGEPRSATVVALTDSELL 75

                          90
                  ....*....|.
gi 47132585   375 AMDVQAFERLL 385
Cdd:pfam00027  76 VIPREDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 277-406 3.65e-15

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: 73.87  E-value: 3.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 277 LKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMkrkgkseVEENGA-VEIARCSRGQYFGELAL 355
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYR-------ISEDGReQILGFLGPGDFFGELSL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47132585 356 VTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVAL 406
Cdd:COG0664  74 LGGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQL 124
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 8-44 5.43e-13

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: 62.74  E-value: 5.43e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 47132585      8 GLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENE 44
Cdd:smart00394   2 GLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
8-43 6.00e-13

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 62.72  E-value: 6.00e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47132585     8 GLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQEN 43
Cdd:pfam02197   2 GLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 172-259 2.77e-12

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: 62.24  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   172 EKLVKDGEHVIDQGDDGDNFYVIDRGTFDIY-VKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRV 250
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYrTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 47132585   251 TFRRIIVKN 259
Cdd:pfam00027  81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 155-274 1.68e-11

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 63.08  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 155 FKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKC-DGVGRCVGNYDNRGSFGELALMYNTPRA 233
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGREQILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132585 234 ATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESL 274
Cdd:COG0664  81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 288-367 2.43e-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: 46.04  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   288 VVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEEngAVEIARCSRGQYFGELALVTNKPRAASAHA 367
Cdd:TIGR03896   4 MVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTR--AFELARLSRGEIVGEMSLLETRPPVATIKA 81
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 154-267 2.00e-26

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: 102.40  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 154 LFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVK-CDGVGRCVGNYDNRGSFGELALMYNTPR 232
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdEDGREQIVGFLGPGDLFGELALLGNGPR 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47132585 233 AATITATSPGALWGLDRVTFRRIIVKNNAKKRKMY 267
Cdd:cd00038  81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 276-396 2.38e-26

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: 102.40  E-value: 2.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 276 FLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEengaveIARCSRGQYFGELAL 355
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQI------VGFLGPGDLFGELAL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132585 356 VTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNI 396
Cdd:cd00038  75 LGNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 154-272 6.86e-24

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: 95.55  E-value: 6.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585    154 LFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVK-CDGVGRCVGNYDNRGSFGELALMYNTPR 232
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVlEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 47132585    233 AATITATSPGaLWGLDRVTFRRIIVKNNAKKRKMYESFIE 272
Cdd:smart00100  81 AASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 276-399 1.62e-23

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: 94.78  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585    276 FLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITmkrkgkSEVEENGAVEIARCSRGQYFGELAL 355
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY------KVLEDGEEQIVGTLGPGDFFGELAL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 47132585    356 VTNKPRAASAHAIGT--VKCLAMDVQAFERLLGPCMEIMKRNIATY 399
Cdd:smart00100  75 LTNSRRAASAAAVALelATLLRIDFRDFLQLLPELPQLLLELLLEL 120
DD_RIIbeta_PKA cd12104
dimerization/docking (D/D) domain of the Type II beta Regulatory subunit of cAMP-dependent ...
 3-45 5.40e-23

dimerization/docking (D/D) domain of the Type II 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIbeta plays an important role in adipocytes and neuronal tissues. Mice deficient with RIIbeta have small fat cells, and are resistant to obesity, diet-induced diabetes, and alcohol-induced motor defects. 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: 438525  Cd Length: 43  Bit Score: 90.73  E-value: 5.40e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 47132585   3 IEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENER 45
Cdd:cd12104   1 IEIPEGLTELLQGFTVEVLRNQPGDLLEFALQYFTRLKQAQSK 43
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 295-385 3.66e-18

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: 78.81  E-value: 3.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   295 KVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEengaveIARCSRGQYFGELALVTNKPRAASAHAIGTVKCL 374
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI------LAVLGPGDFFGELALLGGEPRSATVVALTDSELL 75

                          90
                  ....*....|.
gi 47132585   375 AMDVQAFERLL 385
Cdd:pfam00027  76 VIPREDFLELL 86
DD_RIIalpha_PKA cd12103
dimerization/docking (D/D) domain of the Type II alpha Regulatory subunit of cAMP-dependent ...
 3-42 1.45e-17

dimerization/docking (D/D) domain of the Type II 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. It is also involved in endosome-to-Golgi and Golgi-to-ER transport. 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: 438524  Cd Length: 41  Bit Score: 75.64  E-value: 1.45e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47132585   3 IEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd12103   1 IQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREA 40
DD_RII_PKA cd12099
dimerization/docking (D/D) domain of the Type II Regulatory subunit of cAMP-dependent protein ...
 5-41 2.80e-15

dimerization/docking (D/D) domain of the Type II 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. RIIbeta plays an important role in adipocytes and neuronal tissues. 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: 438520  Cd Length: 37  Bit Score: 69.04  E-value: 2.80e-15
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 47132585   5 IPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQ 41
Cdd:cd12099   1 VPPGLTELLQDFTVAVLREQPTDLVDFAAEYFTRLRE 37
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 277-406 3.65e-15

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: 73.87  E-value: 3.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 277 LKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMkrkgkseVEENGA-VEIARCSRGQYFGELAL 355
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYR-------ISEDGReQILGFLGPGDFFGELSL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47132585 356 VTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVAL 406
Cdd:COG0664  74 LGGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQL 124
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 8-44 5.43e-13

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: 62.74  E-value: 5.43e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 47132585      8 GLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENE 44
Cdd:smart00394   2 GLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
8-43 6.00e-13

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 62.72  E-value: 6.00e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47132585     8 GLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQEN 43
Cdd:pfam02197   2 GLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 172-259 2.77e-12

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: 62.24  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   172 EKLVKDGEHVIDQGDDGDNFYVIDRGTFDIY-VKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRV 250
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYrTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 47132585   251 TFRRIIVKN 259
Cdd:pfam00027  81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 155-274 1.68e-11

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 63.08  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585 155 FKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKC-DGVGRCVGNYDNRGSFGELALMYNTPRA 233
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGREQILGFLGPGDFFGELSLLGGEPSP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132585 234 ATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESL 274
Cdd:COG0664  81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
DD_RII_PKA-like cd12084
dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein ...
 5-40 7.92e-11

dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein kinase and similar domains; 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. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. RI and RII subunits are distinguished by their IS; RII subunits contain a phosphorylation site and are both substrates and inhibitors while RI subunits are pseudo-substrates. RI subunits require ATP and Mg ions to form a stable holoenzyme while RII subunits do not. 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: 438517  Cd Length: 36  Bit Score: 56.66  E-value: 7.92e-11
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 47132585   5 IPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQ 40
Cdd:cd12084   1 VPEGLRELLEDFTREVLREQPEDVYEFAADYFEKLL 36
DD_CrRSP7-like cd22984
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 2-42 9.97e-10

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP7 is a cAMP-dependent protein kinase (PKA) RII-like protein. RSP7 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP7 heterodimerizes with the D/D domain of RSP11 to form an X-type four-helix bundle within the radial spoke RS1 complex.


Pssm-ID: 438553  Cd Length: 47  Bit Score: 53.75  E-value: 9.97e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 47132585   2 SIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd22984   7 KYTIPEEFPAILKDFAREVLREQPKDIYEFGAQYFKRLAEA 47
DD_ROP-like cd22972
dimerization/docking (D/D) domain found in the ropporin (ROP)-like subfamily; The ROP-like ...
 2-42 7.26e-09

dimerization/docking (D/D) domain found in the ropporin (ROP)-like subfamily; The ROP-like family includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP), as well as Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP7 and RSP11. ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. RSP7 is a PKA RII-like protein. RSP11 is a non-PKA RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA.


Pssm-ID: 438541  Cd Length: 43  Bit Score: 51.14  E-value: 7.26e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 47132585   2 SIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd22972   3 QIVIPEGLPEILKAYAKEAIRSQPEDLIQWSAKYFRALADQ 43
DD_CABYR_SP17 cd12100
dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding ...
 5-42 1.35e-08

dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding tYrosine-phosphorylation Regulated protein and Sperm Protein 17; CABYR and SP17 are naturally located in the human sperm fibrous sheath (FS). CABYR was originally isolated from spermatoza and was thought to be testis-specific, but has recently been observed in lung and brain tumors. It is a polymorphic calcium binding protein that is phosphorylated during capacitation. SP17 plays an important role in the interaction of sperm with the zona pellucida during fertilization. It also promotes cell-cell adhesion. SP17 is found in various human tumors of unrelated histological origin including metastatic squamous cell carcinoma, multiple myeloma, ovarian cancer, and primary nervous system tumors, among others. Both CABYR and SP17 contain an N-terminal dimerization/docking (D/D) domain with similarity to the D/D domain of the R subunit of cAMP-dependent protein kinase (PKA). The D/D domain of the R subunit 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. The D/D domain of CABYR and SP17 have been shown to bind to AKAP3, a protein that is also associated to the FS of mammalian spermatozoa.


Pssm-ID: 438521  Cd Length: 42  Bit Score: 50.53  E-value: 1.35e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 47132585   5 IPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd12100   4 LPYGLKSLLEGLSREVLREQPEDIPEFAADYFEELLKF 41
DD_CrRSP11-like cd22985
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 3-42 6.42e-08

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 11 (RSP11) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP11 is a non-PKA (cAMP-dependent protein kinase) RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. RSP11 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP11 heterodimerizes with the D/D domain of RSP7 to form an X-type four-helix bundle within the radial spoke RS1 complex.


Pssm-ID: 438554  Cd Length: 49  Bit Score: 48.71  E-value: 6.42e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47132585   3 IEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd22985   9 INIPPELPDILKNYTKEVIRAQPADLYEFSAEYFAKLAKE 48
DD_R_ScPKA-like cd12098
dimerization/docking (D/D) domain found in Saccharomyces cerevisiae cAMP-dependent protein ...
 5-46 1.78e-05

dimerization/docking (D/D) domain found in Saccharomyces cerevisiae cAMP-dependent protein kinase regulatory subunit and similar domains; 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. The R subunit of fungal PKA is encoded by a single gene, which is called by various names in different organisms (for example: Yarrowia lipolytica RKA1, Saccharomyces cerevisiae Bcy1, and Schizosaccharomyces pombe Cgs1). Although most characterized PKA holoenzymes are tetramers, Y. lipolytica PKA has been reported to be a dimer of RKA1 and the catalytic subunit TPK1. RKA1 is essential and promotes hyphal growth. Cgs1 is essential for sexual differentiation of S. pombe; mutants with defective Cgs1 are partially sterile. 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 of metazoan R subunits dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). The D/D domain of fungal R subunits may also serve as a dimerization domain, in the case of heterotetrameric PKAs. Fungal PKA plays a major role in controlling cell growth and metabolism in response to nutrients and stress conditions.


Pssm-ID: 438519  Cd Length: 45  Bit Score: 41.75  E-value: 1.78e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 47132585   5 IPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRlQQENERK 46
Cdd:cd12098   1 LPSEYPDELNELNREVLRAQPDDILQFCANYFNR-KLEEQRA 41
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 288-367 2.43e-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: 46.04  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132585   288 VVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEEngAVEIARCSRGQYFGELALVTNKPRAASAHA 367
Cdd:TIGR03896   4 MVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTR--AFELARLSRGEIVGEMSLLETRPPVATIKA 81
DD_ROP cd23019
dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A ...
 1-42 2.95e-05

dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP). ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA, which dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). ROP1A and ROP1B have been shown to bind AKAP3.


Pssm-ID: 438555  Cd Length: 43  Bit Score: 41.12  E-value: 2.95e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 47132585   1 MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQE 42
Cdd:cd23019   2 QQINIPPELPDILKQFTKAAIRTQPKDLLQWSAAYFRALSKG 43
DD_RIIAD1 cd22971
dimerization/docking (D/D) domain found in RIIa domain-containing protein 1 (RIIAD1) and ...
 12-38 1.51e-03

dimerization/docking (D/D) domain found in RIIa domain-containing protein 1 (RIIAD1) and similar proteins; The family includes uncharacterized RIIa domain-containing protein 1 (RIIAD1), which contains a C-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: 438540  Cd Length: 41  Bit Score: 36.23  E-value: 1.51e-03
                        10        20
                ....*....|....*....|....*..
gi 47132585  12 LLQGFTVEVLRHQPADLLEFALQHFTR 38
Cdd:cd22971   9 LISGFLREVLKKKPENIREFAAEFFTD 35
DD_CATIP cd22973
dimerization/docking (D/D) domain found in ciliogenesis-associated TTC17-interacting protein ...
 9-37 7.53e-03

dimerization/docking (D/D) domain found in ciliogenesis-associated TTC17-interacting protein (CATIP) and similar proteins; CATIP, also called C2orf62, plays a role in primary ciliogenesis by modulating actin polymerization. It interacts with TTC17. Mutations in CATIP may contribute to asthenozoospermia through its involvement in actin polymerization and the actin cytoskeleton. CATIP contains a C-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: 438542  Cd Length: 40  Bit Score: 33.98  E-value: 7.53e-03
                        10        20
                ....*....|....*....|....*....
gi 47132585   9 LTELLQGFTVEVLRHQPADLLEFALQHFT 37
Cdd:cd22973   9 LKAILSDFLQALLLRKPEDVYQFAAEYFS 37
 
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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