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Conserved domains on  [gi|62822254|gb|AAY14803|]
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unknown, partial [Homo sapiens]

Protein Classification

3',5'-cyclic nucleotide phosphodiesterase( domain architecture ID 10637639)

3',5'-cyclic nucleotide phosphodiesterase catalyzes the hydrolysis of cAMP or cGMP to produce adenosine 5'-phosphate or guanosine 5'-phosphate, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
207-325 5.64e-64

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 202.40  E-value: 5.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254   207 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 286
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 62822254   287 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYF 325
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHF 119
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 15-112 3.29e-16

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


:

Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 74.34  E-value: 3.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254     15 INNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAF 94
Cdd:smart00065  54 LDEGLAGRVAETGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQAL 131

                           90
                   ....*....|....*...
gi 62822254     95 VIFCGLGINNTIMYDQVK 112
Cdd:smart00065 132 ANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
207-325 5.64e-64

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 202.40  E-value: 5.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254   207 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 286
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 62822254   287 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYF 325
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHF 119
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 15-112 3.29e-16

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 74.34  E-value: 3.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254     15 INNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAF 94
Cdd:smart00065  54 LDEGLAGRVAETGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQAL 131

                           90
                   ....*....|....*...
gi 62822254     95 VIFCGLGINNTIMYDQVK 112
Cdd:smart00065 132 ANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 23-102 4.90e-12

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 62.50  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254    23 VASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 102
Cdd:pfam01590  57 VLRTGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
15-118 5.09e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.76  E-value: 5.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254  15 INNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIGVAQVLNRLDGkPFDDADQRLFEA 93
Cdd:COG2203 258 LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIGVLALYSKEPR-AFTEEDLELLEA 335

                        90       100
                ....*....|....*....|....*
gi 62822254  94 FVIFCGLGINNTIMYDQVKKSWAKQ 118
Cdd:COG2203 336 LADQAAIAIERARLYEALEAALAAL 360
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 207-303 1.17e-09

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 55.38  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254    207 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 286
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65

                           90
                   ....*....|....*..
gi 62822254    287 MILQSEGHNIFANLSSK 303
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 207-292 7.11e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 7.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254 207 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 286
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65


                ....*.
gi 62822254 287 MILQSE 292
Cdd:cd00077  66 EILREL 71
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
207-325 5.64e-64

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 202.40  E-value: 5.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254   207 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 286
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 62822254   287 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYF 325
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHF 119
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 15-112 3.29e-16

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 74.34  E-value: 3.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254     15 INNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAF 94
Cdd:smart00065  54 LDEGLAGRVAETGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQAL 131

                           90
                   ....*....|....*...
gi 62822254     95 VIFCGLGINNTIMYDQVK 112
Cdd:smart00065 132 ANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 23-102 4.90e-12

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 62.50  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254    23 VASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 102
Cdd:pfam01590  57 VLRTGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
15-118 5.09e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.76  E-value: 5.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254  15 INNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIGVAQVLNRLDGkPFDDADQRLFEA 93
Cdd:COG2203 258 LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIGVLALYSKEPR-AFTEEDLELLEA 335

                        90       100
                ....*....|....*....|....*
gi 62822254  94 FVIFCGLGINNTIMYDQVKKSWAKQ 118
Cdd:COG2203 336 LADQAAIAIERARLYEALEAALAAL 360
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 207-303 1.17e-09

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 55.38  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254    207 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 286
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65

                           90
                   ....*....|....*..
gi 62822254    287 MILQSEGHNIFANLSSK 303
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
18-112 4.62e-09

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 55.29  E-value: 4.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254  18 SIAELVASTGLPVNISDAYQDPRFdAEADQISGFHIRSVLCVPIwNSNHQIIGVAQVLNRlDGKPFDDADQRLFEAFVIF 97
Cdd:COG3605  74 GLVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPI-IRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQ 150

                        90
                ....*....|....*
gi 62822254  98 CGLGINNTIMYDQVK 112
Cdd:COG3605 151 LAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 207-292 7.11e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 7.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254 207 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 286
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65


                ....*.
gi 62822254 287 MILQSE 292
Cdd:cd00077  66 EILREL 71
GAF_3 pfam13492
GAF domain;
37-94 2.90e-04

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 40.05  E-value: 2.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62822254    37 QDPRFDAEADQISGFHIRSVLCVPIwNSNHQIIGVAqVLNRLDGKPFDDADQRLFEAF 94
Cdd:pfam13492  64 GEPISGLGSAGEDGLPDGPALVVPL-VAGRRVIGVL-ALASSKPRAFDAEDLRLLESL 119
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
 23-95 3.59e-04

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 40.20  E-value: 3.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62822254  23 VASTGLPVNISDAYQDPRfdaeadqisgfHI------RSVLCVPIWNsNHQIIGV----AQVLNRldgkpFDDADQRLFE 92
Cdd:COG1956  82 AAAEGETQLVPDVHAFPG-----------HIacdsasRSEIVVPIFK-DGEVIGVldidSPTPGR-----FDEEDQAGLE 144


                ...
gi 62822254  93 AFV 95
Cdd:COG1956 145 ALA 147
 
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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