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Conserved domains on  [gi|258613973|ref|NP_001158232|]
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cAMP-dependent protein kinase type I-beta regulatory subunit [Homo sapiens]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10186673)

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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD_RIbeta_PKA cd12102
dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent ...
 11-64 5.70e-32

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: 114.65  E-value: 5.70e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258613973  11 EDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQ 64
Cdd:cd12102    1 EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ 54
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 255-370 1.84e-31

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 115.50  E-value: 1.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 255 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 334
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 258613973 335 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 370
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 1.64e-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: 110.11  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 137 LFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 211
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 258613973 212 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 246
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
DD_RIbeta_PKA cd12102
dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent ...
 11-64 5.70e-32

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: 114.65  E-value: 5.70e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258613973  11 EDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQ 64
Cdd:cd12102    1 EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ 54
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 255-370 1.84e-31

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 115.50  E-value: 1.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 255 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 334
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 258613973 335 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 370
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 1.64e-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: 110.11  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 137 LFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 211
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 258613973 212 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 246
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 255-373 2.05e-26

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: 102.09  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973   255 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 332
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 258613973   333 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 373
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-251 2.52e-26

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: 101.71  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973   137 LFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 211
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 258613973   212 AATVKAKTdLKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 251
Cdd:smart00100  81 AASAAAVA-LELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 273-359 1.54e-20

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 84.97  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  273 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 352
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 258613973  353 PRFERVL 359
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 256-359 2.73e-17

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 79.65  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 256 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 335
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 258613973 336 AATVVARGPLKCVKLDRPRFERVL 359
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 160-236 7.54e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 74.95  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  160 AGETVIQQGNEGDNFYVVDQGEVDVYV---NGEWVT--NISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRI 234
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRtleDGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 258613973  235 LM 236
Cdd:pfam00027  86 LE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-235 2.57e-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: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 138 FAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRA 212
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|...
gi 258613973 213 ATVKAKTDLKLWGIDRDSYRRIL 235
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELL 103
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
25-61 7.76e-11

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 56.56  E-value: 7.76e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 258613973   25 HGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEE 61
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 248-350 1.52e-10

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.05  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 248 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 327
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                         90       100
                 ....*....|....*....|...
gi 258613973 328 aLLLNRPRAATVVARGPLKCVKL 350
Cdd:PLN02868  85 -GLSGSVHSADVVAVSELTCLVL 106
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 25-61 1.73e-10

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: 55.42  E-value: 1.73e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 258613973    25 HGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEE 61
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQR 37
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 136-235 4.28e-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: 44.89  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  136 VLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-P 210
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 258613973  211 RAATVKAKTDLKLWGIDRDSYRRIL 235
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 274-341 4.64e-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: 44.89  E-value: 4.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613973  274 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 341
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
163-243 2.44e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 163 TVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 232
Cdd:PRK11753  30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                         90
                 ....*....|....*.
gi 258613973 233 ---RILM--GSTLRKR 243
Cdd:PRK11753 110 vnpDILMalSAQMARR 125
 
Name Accession Description Interval E-value
DD_RIbeta_PKA cd12102
dimerization/docking (D/D) domain of the Type I beta Regulatory subunit of cAMP-dependent ...
 11-64 5.70e-32

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: 114.65  E-value: 5.70e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258613973  11 EDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQ 64
Cdd:cd12102    1 EDESLKGCELYVQKHNIQQILKECIVNLCIAKPDRPMKFLREHFEKLEKEECKQ 54
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 255-370 1.84e-31

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 115.50  E-value: 1.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 255 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRP 334
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY-KLDEDGREQIVGFLGPGDLFGELALLGNGP 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 258613973 335 RAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNI 370
Cdd:cd00038   80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-246 1.64e-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: 110.11  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 137 LFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 211
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 258613973 212 AATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMY 246
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 255-373 2.05e-26

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: 102.09  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973   255 ILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEyVEVGRLGPSDYFGEIALLLN-- 332
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNsr 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 258613973   333 RPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRY 373
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-251 2.52e-26

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: 101.71  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973   137 LFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELALIYGTPR 211
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 258613973   212 AATVKAKTdLKLWGIDRDSYRRILMGSTLRKRKMYEEFLS 251
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 ...
 15-63 2.59e-24

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: 94.14  E-value: 2.59e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 258613973  15 LKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENR 63
Cdd:cd12097    1 LKECEAYIQKHNIQQLLKDCIVQLCVDRPDNPVAFLREYFEKLEKESTR 49
DD_RIalpha_PKA cd12101
dimerization/docking (D/D) domain of the Type I alpha Regulatory subunit of cAMP-dependent ...
 14-63 8.72e-24

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: 92.70  E-value: 8.72e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 258613973  14 SLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENR 63
Cdd:cd12101    1 SLRECELYVQKHNIQQLLKDCIVQLCTARPERPMAFLREYFERLEKEEAK 50
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 273-359 1.54e-20

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 84.97  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  273 PVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDR 352
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVY-RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 258613973  353 PRFERVL 359
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 256-359 2.73e-17

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 79.65  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 256 LESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEVGRLGPSDYFGEIALLLNRPR 335
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLY-RISEDGREQILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 258613973 336 AATVVARGPLKCVKLDRPRFERVL 359
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 160-236 7.54e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 74.95  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  160 AGETVIQQGNEGDNFYVVDQGEVDVYV---NGEWVT--NISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRI 234
Cdd:pfam00027   6 AGEVIFREGDPADSLYIVLSGKVKVYRtleDGREQIlaVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLEL 85


                  ..
gi 258613973  235 LM 236
Cdd:pfam00027  86 LE 87
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-235 2.57e-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: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 138 FAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEW-----VTNISEGGSFGELALIYGTPRA 212
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgreqiLGFLGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|...
gi 258613973 213 ATVKAKTDLKLWGIDRDSYRRIL 235
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELL 103
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
25-61 7.76e-11

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 56.56  E-value: 7.76e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 258613973   25 HGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEE 61
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKLEEER 37
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 248-350 1.52e-10

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 62.05  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 248 EFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLqRRSPNEEYVEvGRLGPSDYFGEi 327
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVS-GPAEEESRPE-FLLKRYDYFGY- 84

                         90       100
                 ....*....|....*....|...
gi 258613973 328 aLLLNRPRAATVVARGPLKCVKL 350
Cdd:PLN02868  85 -GLSGSVHSADVVAVSELTCLVL 106
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 25-61 1.73e-10

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: 55.42  E-value: 1.73e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 258613973    25 HGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEE 61
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKLEEQR 37
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 15-57 1.42e-06

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: 44.72  E-value: 1.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 258613973  15 LKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKL 57
Cdd:cd22961    1 LEDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 136-235 4.28e-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: 44.89  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  136 VLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGE--VDVYVNGEW--VTNISEGGSFGELALIYGT-P 210
Cdd:TIGR03896 144 FIFGELHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEasLSISPDGPGreVGSSRRGEILGETPFLNGSlP 223

                          90       100
                  ....*....|....*....|....*
gi 258613973  211 RAATVKAKTDLKLWGIDRDSYRRIL 235
Cdd:TIGR03896 224 GTATVKAIENSVLLAIDKQQLAAKL 248
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 274-341 4.64e-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: 44.89  E-value: 4.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258613973  274 VQFE--DGEKIVVQGEPGDDFYIITEGTASV---LQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVA 341
Cdd:TIGR03896   9 HQREiaAGTTLIEEGKAADFLFILLDGTFTVttpQPEDNPLTRAFELARLSRGEIVGEMSLLETRPPVATIKA 81
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 19-57 5.49e-05

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: 40.16  E-value: 5.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 258613973  19 ELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKL 57
Cdd:cd22976    5 EEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKL 43
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 160-352 6.46e-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: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  160 AGETVIQQGNEGDNFYVVDQGEVDVYVNGEW---------VTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDS 230
Cdd:TIGR03896  15 AGTTLIEEGKAADFLFILLDGTFTVTTPQPEdnpltrafeLARLSRGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVGE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973  231 YRRILMGSTLRKRKMYEEFLSKVS-----------------------ILESLEKWERLTVA---DALEPVQFEDGEKIVV 284
Cdd:TIGR03896  95 LAAKLQSDVGFAAHFYRAIAIKLAlqiqnqnhqlhrrngadseplrkVLFIFGELHESDVAwmmASGTPQKLPAGTILIH 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613973  285 QGEPGDDFYIITEGTASVLQrrSPNEEYVEVGRLGPSDYFGEIALL-LNRPRAATVVARGPLKCVKLDR 352
Cdd:TIGR03896 175 EGGTVDALYILLYGEASLSI--SPDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLLAIDK 241
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
282-366 1.31e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 42.66  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 282 IVVQGEPGDDFYIITEGTASVLQRRSPNEEYVeVGRLGPSDYFGEIALLL-NRPRAATVVARGPLKCVKLDRPRFERVLG 360
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMI-LSYLNQGDFIGELGLFEeGQERSAWVRAKTACEVAEISYKKFRQLIQ 109


                 ....*.
gi 258613973 361 PCSEIL 366
Cdd:PRK11753 110 VNPDIL 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 280-338 2.51e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 2.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 258613973 280 EKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVevGRLGPSDYFGEIALLLNRPRAAT 338
Cdd:PLN03192 406 EDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVV--GTLGCGDIFGEVGALCCRPQSFT 462
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 21-56 1.24e-03

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: 36.24  E-value: 1.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 258613973  21 YVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEK 56
Cdd:cd22981    8 YLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
163-243 2.44e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613973 163 TVIQQGNEGDNFYVVDQGEVDVYVNGE-----WVTNISEGGSFGELAL-IYGTPRAATVKAKTDLKLWGIDRDSYR---- 232
Cdd:PRK11753  30 TLIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLfEEGQERSAWVRAKTACEVAEISYKKFRqliq 109

                         90
                 ....*....|....*.
gi 258613973 233 ---RILM--GSTLRKR 243
Cdd:PRK11753 110 vnpDILMalSAQMARR 125
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 19-56 3.32e-03

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


Pssm-ID: 438548  Cd Length: 45  Bit Score: 35.13  E-value: 3.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 258613973  19 ELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEK 56
Cdd:cd22979    7 AAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
DD_AtENO3-like cd22962
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ...
 21-57 3.84e-03

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: 34.87  E-value: 3.84e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 258613973  21 YVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKL 57
Cdd:cd22962    6 YLEKHKLEEKLEEAVNAVVKEKPEDPFGFLAQLLRKR 42
 
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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