NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|194390286|dbj|BAG61905|]
View 

unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 103-185 7.02e-21

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: 83.53  E-value: 7.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286 103 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 177
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80


                 ....*...
gi 194390286 178 TATVKSKT 185
Cdd:cd00038   81 SATVRALT 88
DD_cGKI-alpha cd12085
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic ...
 2-49 1.42e-17

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-alpha specifically binds to myosin light chain phosphatase targeting subunit (MYPT1) and the regulator of G-protein signaling-2 (RGS-2). cGKI-alpha activates the phosphatase activity of MYPT1, resulting in vasorelaxation. It increases the activity of RGS-2 toward G proteins, with implications in the downstream signaling for vasoconstrictive agents.


:

Pssm-ID: 213374 [Multi-domain]  Cd Length: 48  Bit Score: 73.08  E-value: 1.42e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 194390286   2 SELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPV 49
Cdd:cd12085    1 SGSVEELQKLLQAKEERIRELEQLLQQRDEEIQELRSQLDKFQSVFPF 48
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 103-185 7.02e-21

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: 83.53  E-value: 7.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286 103 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 177
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80


                 ....*...
gi 194390286 178 TATVKSKT 185
Cdd:cd00038   81 SATVRALT 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 103-185 1.23e-20

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: 83.22  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286   103 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTK-----EGVKLCTMGPGKVFGELAILYNCTR 177
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSRR 80


                   ....*...
gi 194390286   178 TATVKSKT 185
Cdd:smart00100  81 AASAAAVA 88
DD_cGKI-alpha cd12085
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic ...
 2-49 1.42e-17

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-alpha specifically binds to myosin light chain phosphatase targeting subunit (MYPT1) and the regulator of G-protein signaling-2 (RGS-2). cGKI-alpha activates the phosphatase activity of MYPT1, resulting in vasorelaxation. It increases the activity of RGS-2 toward G proteins, with implications in the downstream signaling for vasoconstrictive agents.


Pssm-ID: 213374 [Multi-domain]  Cd Length: 48  Bit Score: 73.08  E-value: 1.42e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 194390286   2 SELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPV 49
Cdd:cd12085    1 SGSVEELQKLLQAKEERIRELEQLLQQRDEEIQELRSQLDKFQSVFPF 48
PKcGMP_CC pfam16808
Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal ...
 10-44 2.87e-12

Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal coiled-coil, dimerization, domain of cGMP-protein kinases.


Pssm-ID: 465276  Cd Length: 35  Bit Score: 58.94  E-value: 2.87e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 194390286   10 KILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQ 44
Cdd:pfam16808   1 KILRLKDERIRELEKRLAEKDEEIQELKSKLDKYQ 35
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 121-194 1.45e-11

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: 58.39  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286  121 PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRTATVKSKT----IFIFLK 191
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEPRSATVVALTdselLVIPRE 80


                  ...
gi 194390286  192 YFQ 194
Cdd:pfam00027  81 DFL 83
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 104-181 2.80e-08

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: 51.91  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286 104 MKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRT 178
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEPSP 80


                 ...
gi 194390286 179 ATV 181
Cdd:COG0664   81 ATA 83
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
15-40 8.32e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 8.32e-03
                         10        20
                 ....*....|....*....|....*.
gi 194390286  15 KEERIKELEKRLSEKEEEIQELKRKL 40
Cdd:COG2433  470 LDREIERLERELEEERERIEELKRKL 495
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 103-185 7.02e-21

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: 83.53  E-value: 7.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286 103 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 177
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80


                 ....*...
gi 194390286 178 TATVKSKT 185
Cdd:cd00038   81 SATVRALT 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 103-185 1.23e-20

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: 83.22  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286   103 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTK-----EGVKLCTMGPGKVFGELAILYNCTR 177
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSRR 80


                   ....*...
gi 194390286   178 TATVKSKT 185
Cdd:smart00100  81 AASAAAVA 88
DD_cGKI-alpha cd12085
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic ...
 2-49 1.42e-17

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-alpha specifically binds to myosin light chain phosphatase targeting subunit (MYPT1) and the regulator of G-protein signaling-2 (RGS-2). cGKI-alpha activates the phosphatase activity of MYPT1, resulting in vasorelaxation. It increases the activity of RGS-2 toward G proteins, with implications in the downstream signaling for vasoconstrictive agents.


Pssm-ID: 213374 [Multi-domain]  Cd Length: 48  Bit Score: 73.08  E-value: 1.42e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 194390286   2 SELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPV 49
Cdd:cd12085    1 SGSVEELQKLLQAKEERIRELEQLLQQRDEEIQELRSQLDKFQSVFPF 48
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 2-49 1.61e-15

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373 [Multi-domain]  Cd Length: 48  Bit Score: 67.59  E-value: 1.61e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 194390286   2 SELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPV 49
Cdd:cd12083    1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQSVLPP 48
PKcGMP_CC pfam16808
Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal ...
 10-44 2.87e-12

Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal coiled-coil, dimerization, domain of cGMP-protein kinases.


Pssm-ID: 465276  Cd Length: 35  Bit Score: 58.94  E-value: 2.87e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 194390286   10 KILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQ 44
Cdd:pfam16808   1 KILRLKDERIRELEKRLAEKDEEIQELKSKLDKYQ 35
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 121-194 1.45e-11

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: 58.39  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286  121 PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRTATVKSKT----IFIFLK 191
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEPRSATVVALTdselLVIPRE 80


                  ...
gi 194390286  192 YFQ 194
Cdd:pfam00027  81 DFL 83
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 104-181 2.80e-08

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: 51.91  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390286 104 MKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRT 178
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEPSP 80


                 ...
gi 194390286 179 ATV 181
Cdd:COG0664   81 ATA 83
DD_cGKI-beta cd12086
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta; Cyclic ...
 12-47 3.57e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing for their targeting to different subcellular compartments and intracellular substrates. cGKI-beta binds specifically to inositol triphosphate receptor-associated PKG substrate (IRAG) and the transcriptional regulator TFII-I. Phosphorylation of IRAG by cGKI-beta contributes to smooth muscle relaxation while phosphorylation of TFII-I modulates its co-activator functions for serum response factor and Smad transcription factors.


Pssm-ID: 213375  Cd Length: 52  Bit Score: 34.63  E-value: 3.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 194390286  12 LMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVL 47
Cdd:cd12086   15 LRKRDELIKELEQELDEKDALIQHLQNELDKYRSVV 50
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
15-40 8.32e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 8.32e-03
                         10        20
                 ....*....|....*....|....*.
gi 194390286  15 KEERIKELEKRLSEKEEEIQELKRKL 40
Cdd:COG2433  470 LDREIERLERELEEERERIEELKRKL 495
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
 15-41 8.80e-03

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 33.85  E-value: 8.80e-03
                         10        20
                 ....*....|....*....|....*..
gi 194390286  15 KEERIKELEKRLSEKEEEIQELKRKLH 41
Cdd:cd14688   21 KKERIKELEQRVAELEEELAELEEELQ 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH