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Conserved domains on  [gi|133901990|ref|NP_001076771|]
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cAMP-dependent protein kinase regulatory subunit [Caenorhabditis elegans]

Protein Classification

cyclic nucleotide-binding domain-containing protein; MDR family MFS transporter( domain architecture ID 10186648)

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.| MDR (multi-drug resistance) family major facilitator superfamily (MFS) transporter confers resistance to specific drugs/toxins through their active efflux from the cell

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 ...
 132-241 8.07e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 8.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 132 LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHE-----YVLTINEGGSFGELALIYGTPR 206
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 133901990 207 AATVIAKTDVKLWAIDRLTYRRILMGSVTKKRKMY 241
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 250-363 9.24e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 9.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 250 ILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLqKRSDDAPFDVVGHLGMSDYFGEIALLLDRP 329
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 133901990 330 RAATVVAKTHLKCIKLDRNRFERVMGPVREILKR 363
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARR 113
DD_RI_PKA cd12097
dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein ...
 20-68 3.84e-22

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: 87.98  E-value: 3.84e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 133901990  20 LAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRAQ 68
Cdd:cd12097    1 LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR 49
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 132-241 8.07e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 8.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 132 LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHE-----YVLTINEGGSFGELALIYGTPR 206
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 133901990 207 AATVIAKTDVKLWAIDRLTYRRILMGSVTKKRKMY 241
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 250-363 9.24e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 9.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 250 ILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLqKRSDDAPFDVVGHLGMSDYFGEIALLLDRP 329
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 133901990 330 RAATVVAKTHLKCIKLDRNRFERVMGPVREILKR 363
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARR 113
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 132-246 8.72e-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: 94.78  E-value: 8.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990   132 LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHEY-----VLTINEGGSFGELALIYGTPR 206
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqiVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 133901990   207 AATVIAKTdVKLWAIDRLTYRRILMGSVTKKRKMYDEFLS 246
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
DD_RI_PKA cd12097
dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein ...
 20-68 3.84e-22

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: 87.98  E-value: 3.84e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 133901990  20 LAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRAQ 68
Cdd:cd12097    1 LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR 49
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 250-368 2.14e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 2.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990   250 ILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDApFDVVGHLGMSDYFGEIALLLDRP 329
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGE-EQIVGTLGPGDFFGELALLTNSR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 133901990   330 RAATVVAKTH--LKCIKLDRNRFERVMGPVREILKRDVSNY 368
Cdd:smart00100  80 RAASAAAVALelATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 271-354 2.56e-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: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  271 FEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFdVVGHLGMSDYFGEIALLLDRPRAATVVAKTHLKCIKLDRNRF 350
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQ-ILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDF 82


                  ....
gi 133901990  351 ERVM 354
Cdd:pfam00027  83 LELL 86
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-231 4.37e-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: 78.42  E-value: 4.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  155 AGETIIEQGEEGDNFYVIDKGTVDVYVNHE-----YVLTINEGGSFGELALIYGTPRAATVIAKTDVKLWAIDRLTYRRI 229
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 133901990  230 LM 231
Cdd:pfam00027  86 LE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 133-230 1.18e-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: 77.72  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 133 FAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVN----HEYVLTI-NEGGSFGELALIYGTPRA 207
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIsedgREQILGFlGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|...
gi 133901990 208 ATVIAKTDVKLWAIDRLTYRRIL 230
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELL 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 251-354 2.91e-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: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 251 LADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFdVVGHLGMSDYFGEIALLLDRPR 330
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQ-ILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 133901990 331 AATVVAKTHLKCIKLDRNRFERVM 354
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 30-67 2.65e-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: 60.81  E-value: 2.65e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 133901990    30 HNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRA 67
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
30-66 5.90e-12

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 59.64  E-value: 5.90e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 133901990   30 HNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQR 66
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 243-345 4.16e-09

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 57.81  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 243 EFLSKVQILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFDVVghLGMSDYFGEi 322
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFL--LKRYDYFGY- 84

                         90       100
                 ....*....|....*....|...
gi 133901990 323 aLLLDRPRAATVVAKTHLKCIKL 345
Cdd:PLN02868  85 -GLSGSVHSADVVAVSELTCLVL 106
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
158-231 1.51e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 45.36  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 158 TIIEQGEEGDNFYVIDKGTVDVYV----NHEYVLT-INEGGSFGELAL-IYGTPRAATVIAKTDVKLWAI--DRL----- 224
Cdd:PRK11753  30 TLIHAGEKAETLYYIVKGSVAVLIkdeeGKEMILSyLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEIsyKKFrqliq 109


                 ....*..
gi 133901990 225 TYRRILM 231
Cdd:PRK11753 110 VNPDILM 116
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 256-336 5.88e-05

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


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 44.50  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  256 QWERANVadalERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFDV---VGHLGMSDYFGEIALLLDRPRAA 332
Cdd:TIGR03896   2 DWMVAIG----HQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTRafeLARLSRGEIVGEMSLLETRPPVA 77


                  ....
gi 133901990  333 TVVA 336
Cdd:TIGR03896  78 TIKA 81
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 127-241 1.90e-03

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: 39.88  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  127 MRKNL-LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHE----YVLTINEGGSFGELALI 201
Cdd:TIGR03896 139 LRKVLfIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDgpgrEVGSSRRGEILGETPFL 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 133901990  202 YGT-PRAATVIAKTDVKLWAIDRLTYRRILMGSVTKKRKMY 241
Cdd:TIGR03896 219 NGSlPGTATVKAIENSVLLAIDKQQLAAKLQQDVGFASRFY 259
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 132-241 8.07e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 8.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 132 LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHE-----YVLTINEGGSFGELALIYGTPR 206
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 133901990 207 AATVIAKTDVKLWAIDRLTYRRILMGSVTKKRKMY 241
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 250-363 9.24e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 108.18  E-value: 9.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 250 ILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLqKRSDDAPFDVVGHLGMSDYFGEIALLLDRP 329
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 133901990 330 RAATVVAKTHLKCIKLDRNRFERVMGPVREILKR 363
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARR 113
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 132-246 8.72e-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: 94.78  E-value: 8.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990   132 LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHEY-----VLTINEGGSFGELALIYGTPR 206
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDgeeqiVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 133901990   207 AATVIAKTdVKLWAIDRLTYRRILMGSVTKKRKMYDEFLS 246
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
DD_RI_PKA cd12097
dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein ...
 20-68 3.84e-22

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: 87.98  E-value: 3.84e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 133901990  20 LAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRAQ 68
Cdd:cd12097    1 LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR 49
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 250-368 2.14e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 2.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990   250 ILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDApFDVVGHLGMSDYFGEIALLLDRP 329
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGE-EQIVGTLGPGDFFGELALLTNSR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 133901990   330 RAATVVAKTH--LKCIKLDRNRFERVMGPVREILKRDVSNY 368
Cdd:smart00100  80 RAASAAAVALelATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 271-354 2.56e-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: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  271 FEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFdVVGHLGMSDYFGEIALLLDRPRAATVVAKTHLKCIKLDRNRF 350
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQ-ILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDF 82


                  ....
gi 133901990  351 ERVM 354
Cdd:pfam00027  83 LELL 86
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-231 4.37e-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: 78.42  E-value: 4.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  155 AGETIIEQGEEGDNFYVIDKGTVDVYVNHE-----YVLTINEGGSFGELALIYGTPRAATVIAKTDVKLWAIDRLTYRRI 229
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 133901990  230 LM 231
Cdd:pfam00027  86 LE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 133-230 1.18e-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: 77.72  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 133 FAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVN----HEYVLTI-NEGGSFGELALIYGTPRA 207
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIsedgREQILGFlGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|...
gi 133901990 208 ATVIAKTDVKLWAIDRLTYRRIL 230
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELL 103
DD_RIbeta_PKA cd12102
dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent ...
 16-69 5.48e-16

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: 71.51  E-value: 5.48e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 133901990  16 EEDQLAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRAQE 69
Cdd:cd12102    1 EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ 54
DD_RIalpha_PKA cd12101
dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent ...
 20-68 1.27e-15

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: 70.36  E-value: 1.27e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 133901990  20 LAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRAQ 68
Cdd:cd12101    2 LRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK 50
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 251-354 2.91e-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: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 251 LADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFdVVGHLGMSDYFGEIALLLDRPR 330
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQ-ILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 133901990 331 AATVVAKTHLKCIKLDRNRFERVM 354
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 30-67 2.65e-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: 60.81  E-value: 2.65e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 133901990    30 HNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQRA 67
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQRA 38
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
30-66 5.90e-12

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 59.64  E-value: 5.90e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 133901990   30 HNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQR 66
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 243-345 4.16e-09

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 57.81  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 243 EFLSKVQILADLDQWERANVADALERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFDVVghLGMSDYFGEi 322
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFL--LKRYDYFGY- 84

                         90       100
                 ....*....|....*....|...
gi 133901990 323 aLLLDRPRAATVVAKTHLKCIKL 345
Cdd:PLN02868  85 -GLSGSVHSADVVAVSELTCLVL 106
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 20-62 3.09e-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: 46.26  E-value: 3.09e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 133901990  20 LAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKL 62
Cdd:cd22961    1 LEDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 21-66 2.36e-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: 44.01  E-value: 2.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 133901990  21 AQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQR 66
Cdd:cd22976    2 EEAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKLKEAR 47
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
158-231 1.51e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 45.36  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 158 TIIEQGEEGDNFYVIDKGTVDVYV----NHEYVLT-INEGGSFGELAL-IYGTPRAATVIAKTDVKLWAI--DRL----- 224
Cdd:PRK11753  30 TLIHAGEKAETLYYIVKGSVAVLIkdeeGKEMILSyLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEIsyKKFrqliq 109


                 ....*..
gi 133901990 225 TYRRILM 231
Cdd:PRK11753 110 VNPDILM 116
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 17-66 1.63e-05

dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and similar proteins; 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. It contains a C-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: 438544  Cd Length: 50  Bit Score: 41.78  E-value: 1.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 133901990  17 EDQLAQCQAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLNEQR 66
Cdd:cd22975    1 EDPYEKAVKYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEIEKIIKER 50
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 24-61 2.33e-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: 2.33e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 133901990  24 QAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEK 61
Cdd:cd22981    6 QKYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
DD_AtENO3-like cd22962
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ...
 24-62 3.36e-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: 40.64  E-value: 3.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 133901990  24 QAYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKL 62
Cdd:cd22962    4 QEYLEKHKLEEKLEEAVNAVVKEKPEDPFGFLAQLLRKR 42
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 25-61 4.03e-05

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: 40.53  E-value: 4.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 133901990  25 AYVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEK 61
Cdd:cd22979    8 AYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 256-336 5.88e-05

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


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 44.50  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  256 QWERANVadalERCDFEPGTHVVEQGQPGDEFFIILEGEANVLQKRSDDAPFDV---VGHLGMSDYFGEIALLLDRPRAA 332
Cdd:TIGR03896   2 DWMVAIG----HQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTRafeLARLSRGEIVGEMSLLETRPPVA 77


                  ....
gi 133901990  333 TVVA 336
Cdd:TIGR03896  78 TIKA 81
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 273-354 3.00e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990 273 PGTHVVEQGQPGDEFFIILEGEANVLQKRSDDApfDVVGHLGMSDYFGEIALLLDRPRAATVVAKTHLKCIKLDRNRFER 352
Cdd:PLN03192 404 PREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKE--RVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIE 481


                 ..
gi 133901990 353 VM 354
Cdd:PLN03192 482 AM 483
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
 35-62 3.55e-04

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: 37.48  E-value: 3.55e-04
                         10        20
                 ....*....|....*....|....*...
gi 133901990  35 LVKEAIVVLCIHKPDNPVLFLKDHFEKL 62
Cdd:cd22957    2 LLQDAVAKLLEERPEDPVEFLAEYFEKA 29
DD_TPGS1 cd22960
dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) ...
 26-63 1.01e-03

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: 36.42  E-value: 1.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 133901990  26 YVQRHNIQQLVKEAIVVLCIHKPDNPVLFLKDHFEKLN 63
Cdd:cd22960    2 FLERTGVTSLLRDALLKVLENRPEDPIAFLAEYFESLA 39
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 127-241 1.90e-03

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: 39.88  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133901990  127 MRKNL-LFAHLEEDEQKTMYDAMFPVEKSAGETIIEQGEEGDNFYVIDKGTVDVYVNHE----YVLTINEGGSFGELALI 201
Cdd:TIGR03896 139 LRKVLfIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDgpgrEVGSSRRGEILGETPFL 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 133901990  202 YGT-PRAATVIAKTDVKLWAIDRLTYRRILMGSVTKKRKMY 241
Cdd:TIGR03896 219 NGSlPGTATVKAIENSVLLAIDKQQLAAKLQQDVGFASRFY 259
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
275-338 4.12e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.04  E-value: 4.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 133901990 275 THVVEQGQPGDEFFIILEGEANVLQKRSDDAPFdVVGHLGMSDYFGEIALLLD-RPRAATVVAKT 338
Cdd:PRK11753  29 STLIHAGEKAETLYYIVKGSVAVLIKDEEGKEM-ILSYLNQGDFIGELGLFEEgQERSAWVRAKT 92
 
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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