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Conserved domains on  [gi|767963270|ref|XP_011538254|]
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cGMP-dependent protein kinase 1 isoform X2 [Homo sapiens]

Protein Classification

DD_cGKI-beta and CAP_ED domain-containing protein( domain architecture ID 10186558)

DD_cGKI-beta and CAP_ED domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 237-341 3.51e-30

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 112.42  E-value: 3.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDsPSEDPVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLD-EDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100
                 ....*....|....*....|....*
gi 767963270 317 TANVIAAEAVTCLVIDRDSFKHLIG 341
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQ 105
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 118-227 1.40e-27

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: 105.49  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 118 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 192
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767963270 193 TATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEY 227
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
DD_cGKI-beta cd12086
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta; Cyclic ...
 4-55 6.67e-21

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: 85.09  E-value: 6.67e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767963270   4 LRDLQYALQEKIEELRQRDALIDELELELDQKDELIQKLQNELDKYRSVIRP 55
Cdd:cd12086    1 LRDLQRALQEKTEELRKRDELIKELEQELDEKDALIQHLQNELDKYRSVVRP 52
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 237-341 3.51e-30

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 112.42  E-value: 3.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDsPSEDPVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLD-EDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100
                 ....*....|....*....|....*
gi 767963270 317 TANVIAAEAVTCLVIDRDSFKHLIG 341
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQ 105
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 118-227 1.40e-27

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: 105.49  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 118 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 192
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767963270 193 TATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEY 227
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 237-355 2.76e-27

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 104.79  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270   237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDpVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767963270   317 TANViAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAE 355
Cdd:smart00100  81 AASA-AAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 118-222 3.12e-23

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 93.62  E-value: 3.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270   118 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTK-----EGVKLCTMGPGKVFGELAILYNC-- 190
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSrr 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767963270   191 TRTATVKTLVNVKLWAIDRQCFQTIMMRTGLI 222
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQL 112
DD_cGKI-beta cd12086
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta; Cyclic ...
 4-55 6.67e-21

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: 85.09  E-value: 6.67e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767963270   4 LRDLQYALQEKIEELRQRDALIDELELELDQKDELIQKLQNELDKYRSVIRP 55
Cdd:cd12086    1 LRDLQRALQEKTEELRKRDELIKELEQELDEKDALIQHLQNELDKYRSVVRP 52
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 254-340 8.44e-21

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 86.12  E-value: 8.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  254 ETHYENGEYIIRQGARGDTFFIISKGTVNVTReDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDR 333
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYR-TLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 767963270  334 DSFKHLI 340
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 237-340 3.43e-20

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: 88.12  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDsPSEDPVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIS-EDGREQILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 767963270 317 TANVIAAEAVTCLVIDRDSFKHLI 340
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 226-334 1.07e-19

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 90.16  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 226 EYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLrtLGKGDWF 305
Cdd:PLN02868   5 SVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFL--LKRYDYF 82

                         90       100
                 ....*....|....*....|....*....
gi 767963270 306 GEKALQgeDVRTANVIAAEAVTCLVIDRD 334
Cdd:PLN02868  83 GYGLSG--SVHSADVVAVSELTCLVLPHE 109
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 136-218 3.83e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 75.72  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  136 PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQ 210
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*...
gi 767963270  211 CFQTIMMR 218
Cdd:pfam00027  81 DFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 119-218 6.68e-12

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: 64.24  E-value: 6.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 119 MKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRT 193
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|....*
gi 767963270 194 ATVKTLVNVKLWAIDRQCFQTIMMR 218
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLER 105
PKcGMP_CC pfam16808
Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal ...
 16-50 1.21e-09

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: 53.16  E-value: 1.21e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767963270   16 EELRQRDALIDELELELDQKDELIQKLQNELDKYR 50
Cdd:pfam16808   1 KILRLKDERIRELEKRLAEKDEEIQELKSKLDKYQ 35
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
11-54 1.65e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 1.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767963270  11 LQEKIEELRqrdALIDELELELDQKDELIQKLQNELDKYRSVIR 54
Cdd:COG2433  418 LEEQVERLE---AEVEELEAELEEKDERIERLERELSEARSEER 458
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 127-335 3.69e-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: 39.11  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  127 IQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVT---------KEGVKLCTMGPGKVFGELAILYNCTRTATVK 197
Cdd:TIGR03896   1 IDWMVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTtpqpednplTRAFELARLSRGEIVGEMSLLETRPPVATIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  198 TLVNVKLWAIDRQCFQTIMMRTGLIKHTEY--------------MEFLKSVPTFQSLPeeiLSKLADVLEETHYENGEYI 263
Cdd:TIGR03896  81 AVPKSRVMSIPVGELAAKLQSDVGFAAHFYraiaiklalqiqnqNHQLHRRNGADSEP---LRKVLFIFGELHESDVAWM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  264 IRQGARGD----TFFIISKGTVN------------VTREDSPSEDPVFLRtlgKGDWFGEKA-LQGEDVRTANVIAAEAV 326
Cdd:TIGR03896 158 MASGTPQKlpagTILIHEGGTVDalyillygeaslSISPDGPGREVGSSR---RGEILGETPfLNGSLPGTATVKAIENS 234


                  ....*....
gi 767963270  327 TCLVIDRDS 335
Cdd:TIGR03896 235 VLLAIDKQQ 243
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 237-341 3.51e-30

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 112.42  E-value: 3.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDsPSEDPVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLD-EDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100
                 ....*....|....*....|....*
gi 767963270 317 TANVIAAEAVTCLVIDRDSFKHLIG 341
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQ 105
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 118-227 1.40e-27

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: 105.49  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 118 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTR 192
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDedgreQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767963270 193 TATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEY 227
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 237-355 2.76e-27

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 104.79  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270   237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDpVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEE-QIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767963270   317 TANViAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAE 355
Cdd:smart00100  81 AASA-AAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 118-222 3.12e-23

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 93.62  E-value: 3.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270   118 FMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTK-----EGVKLCTMGPGKVFGELAILYNC-- 190
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvledgEEQIVGTLGPGDFFGELALLTNSrr 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767963270   191 TRTATVKTLVNVKLWAIDRQCFQTIMMRTGLI 222
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQL 112
DD_cGKI-beta cd12086
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I beta; Cyclic ...
 4-55 6.67e-21

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: 85.09  E-value: 6.67e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767963270   4 LRDLQYALQEKIEELRQRDALIDELELELDQKDELIQKLQNELDKYRSVIRP 55
Cdd:cd12086    1 LRDLQRALQEKTEELRKRDELIKELEQELDEKDALIQHLQNELDKYRSVVRP 52
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 254-340 8.44e-21

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 86.12  E-value: 8.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  254 ETHYENGEYIIRQGARGDTFFIISKGTVNVTReDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDR 333
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYR-TLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                  ....*..
gi 767963270  334 DSFKHLI 340
Cdd:pfam00027  80 EDFLELL 86
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 237-340 3.43e-20

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: 88.12  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 237 FQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDsPSEDPVFLRTLGKGDWFGEKALQGEDVR 316
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIS-EDGREQILGFLGPGDFFGELSLLGGEPS 79

                         90       100
                 ....*....|....*....|....
gi 767963270 317 TANVIAAEAVTCLVIDRDSFKHLI 340
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELL 103
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 226-334 1.07e-19

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 90.16  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 226 EYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLrtLGKGDWF 305
Cdd:PLN02868   5 SVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFL--LKRYDYF 82

                         90       100
                 ....*....|....*....|....*....
gi 767963270 306 GEKALQgeDVRTANVIAAEAVTCLVIDRD 334
Cdd:PLN02868  83 GYGLSG--SVHSADVVAVSELTCLVLPHE 109
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 136-218 3.83e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 75.72  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  136 PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQ 210
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLedgreQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*...
gi 767963270  211 CFQTIMMR 218
Cdd:pfam00027  81 DFLELLER 88
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 8-55 7.74e-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: 67.98  E-value: 7.74e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767963270   8 QYALQEKIEELRQRDALIDELELELDQKDELIQKLQNELDKYRSVIRP 55
Cdd:cd12083    1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQSVLPP 48
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 119-218 6.68e-12

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: 64.24  E-value: 6.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270 119 MKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEG-----VKLCTMGPGKVFGELAILYNCTRT 193
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISedgreQILGFLGPGDFFGELSLLGGEPSP 80

                         90       100
                 ....*....|....*....|....*
gi 767963270 194 ATVKTLVNVKLWAIDRQCFQTIMMR 218
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLER 105
PKcGMP_CC pfam16808
Coiled-coil N-terminus of cGMP-dependent protein kinase; PKcGMP_CC is the N-terminal ...
 16-50 1.21e-09

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: 53.16  E-value: 1.21e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767963270   16 EELRQRDALIDELELELDQKDELIQKLQNELDKYR 50
Cdd:pfam16808   1 KILRLKDERIRELEKRLAEKDEEIQELKSKLDKYQ 35
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
263-340 7.10e-05

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 43.82  E-value: 7.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767963270 263 IIRQGARGDTFFIISKGTVNVTREDSpSEDPVFLRTLGKGDWFGEKALQGE-DVRTANVIAAEAVTCLVIDRDSFKHLI 340
Cdd:PRK11753  31 LIHAGEKAETLYYIVKGSVAVLIKDE-EGKEMILSYLNQGDFIGELGLFEEgQERSAWVRAKTACEVAEISYKKFRQLI 108
Med28 pfam11594
Mediator complex subunit 28; Mediator is a large complex of up to 33 proteins that is ...
 7-53 8.51e-05

Mediator complex subunit 28; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Subunit Med28 of the Mediator may function as a scaffolding protein within Mediator by maintaining the stability of a submodule within the head module, and components of this submodule act together in a gene-regulatory programme to suppress smooth muscle cell differentiation. Thus, mammalian Mediator subunit Med28 functions as a repressor of smooth muscle-cell differentiation, which could have implications for disorders associated with abnormalities in smooth muscle cell growth and differentiation, including atherosclerosis, asthma, hypertension, and smooth muscle tumours.


Pssm-ID: 463302  Cd Length: 101  Bit Score: 41.48  E-value: 8.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767963270    7 LQYALQEKIEELRQRdalIDELELELDQKDELIQKLQNELDKYRSVI 53
Cdd:pfam11594  58 LLLSAQKPEEVLKEE---IAELRAELERKDELIKKHKEKIQEWQSVL 101
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
11-54 1.65e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 1.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767963270  11 LQEKIEELRqrdALIDELELELDQKDELIQKLQNELDKYRSVIR 54
Cdd:COG2433  418 LEEQVERLE---AEVEELEAELEEKDERIERLERELSEARSEER 458
DD_cGKI-alpha cd12085
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I alpha; Cyclic ...
 1-55 2.08e-04

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: 38.79  E-value: 2.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767963270   1 MGTLRDLQYALQEKIEELRqrdalidELELELDQKDELIQKLQNELDKYRSVIRP 55
Cdd:cd12085    1 SGSVEELQKLLQAKEERIR-------ELEQLLQQRDEEIQELRSQLDKFQSVFPF 48
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 127-335 3.69e-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: 39.11  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  127 IQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVT---------KEGVKLCTMGPGKVFGELAILYNCTRTATVK 197
Cdd:TIGR03896   1 IDWMVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTtpqpednplTRAFELARLSRGEIVGEMSLLETRPPVATIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  198 TLVNVKLWAIDRQCFQTIMMRTGLIKHTEY--------------MEFLKSVPTFQSLPeeiLSKLADVLEETHYENGEYI 263
Cdd:TIGR03896  81 AVPKSRVMSIPVGELAAKLQSDVGFAAHFYraiaiklalqiqnqNHQLHRRNGADSEP---LRKVLFIFGELHESDVAWM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963270  264 IRQGARGD----TFFIISKGTVN------------VTREDSPSEDPVFLRtlgKGDWFGEKA-LQGEDVRTANVIAAEAV 326
Cdd:TIGR03896 158 MASGTPQKlpagTILIHEGGTVDalyillygeaslSISPDGPGREVGSSR---RGEILGETPfLNGSLPGTATVKAIENS 234


                  ....*....
gi 767963270  327 TCLVIDRDS 335
Cdd:TIGR03896 235 VLLAIDKQQ 243
 
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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