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Conserved domains on  [gi|1824718152|ref|NP_001366175|]
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rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta isoform 3 [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;
277-521 4.70e-107

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.04  E-value: 4.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 277 YHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 355
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 356 FLLSEETLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSwveylslETTRKEIVMAMMM 435
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLEN-------EEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 436 TACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTvLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEIL 515
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 1824718152 516 PMFDRL 521
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
52-160 7.38e-19

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: 83.58  E-value: 7.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152   52 PTPSADHWALASGLPSYVAESGFICNIMNASADEmfkFQEGALDDSGWLIKNVLSMPIVNKkEEIVGVATFYNRKDGKPF 131
Cdd:smart00065  45 LPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP---LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPF 120
                           90       100
                   ....*....|....*....|....*....
gi 1824718152  132 DEQDEVLMESLTQFLGWSVMNTDTYDKMN 160
Cdd:smart00065 121 TEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
277-521 4.70e-107

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.04  E-value: 4.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 277 YHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 355
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 356 FLLSEETLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSwveylslETTRKEIVMAMMM 435
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLEN-------EEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 436 TACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTvLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEIL 515
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 1824718152 516 PMFDRL 521
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
52-160 7.38e-19

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: 83.58  E-value: 7.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152   52 PTPSADHWALASGLPSYVAESGFICNIMNASADEmfkFQEGALDDSGWLIKNVLSMPIVNKkEEIVGVATFYNRKDGKPF 131
Cdd:smart00065  45 LPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP---LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPF 120
                           90       100
                   ....*....|....*....|....*....
gi 1824718152  132 DEQDEVLMESLTQFLGWSVMNTDTYDKMN 160
Cdd:smart00065 121 TEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
276-361 9.48e-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: 53.84  E-value: 9.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  276 TYHNWRHGFNVAQTMFTLLMTGKLksyytdLEAFAMVTAGLCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 355
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65

                   ....*.
gi 1824718152  356 FLLSEE 361
Cdd:smart00471  66 ILLEEE 71
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
277-462 3.20e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.03  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 277 YHNWRHGFNVAQTMFTLLMTGKLksyyTDLEAFAMVTAGLCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKF 356
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 357 LLSEETLniyqnlnrrqhEHVIHLMDIAIIATDlALYFKKRAMFQKIVDESKNYQDKkswveylslettrkeivMAMMMT 436
Cdd:cd00077    67 ILRELLL-----------EEVIKLIDELILAVD-ASHHERLDGLGYPDGLKGEEITL-----------------EARIVK 117
                         170       180
                  ....*....|....*....|....*...
gi 1824718152 437 ACDLSAITK--PWEVQSKVALLVAAEFW 462
Cdd:cd00077   118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-150 1.72e-06

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: 47.47  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  53 TPSADHWALASGL------PSYVAESGFICNIMNASADEMFKFQEGALDDSGwlIKNVLSMPIVNKkEEIVGVATFYNRK 126
Cdd:pfam01590  35 LPPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDD-GELLGVLVLHHPR 111
                          90       100
                  ....*....|....*....|....
gi 1824718152 127 DgkPFDEQDEVLMESLTQFLGWSV 150
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
51-165 1.89e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 47.50  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  51 IPTPSADHWALASGLPSYVAESGFICNIMNASADEMF-KFQEGALDDSGwlIKNVLSMPIVNKkEEIVGVATFYNRKDGk 129
Cdd:COG2203   248 LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR- 323
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1824718152 130 PFDEQDEVLMESLTQFLGWSVMNTDTYDKMNKLENR 165
Cdd:COG2203   324 AFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
277-521 4.70e-107

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.04  E-value: 4.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 277 YHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 355
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 356 FLLSEETLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSwveylslETTRKEIVMAMMM 435
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLEN-------EEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 436 TACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTvLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEIL 515
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 1824718152 516 PMFDRL 521
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
52-160 7.38e-19

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: 83.58  E-value: 7.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152   52 PTPSADHWALASGLPSYVAESGFICNIMNASADEmfkFQEGALDDSGWLIKNVLSMPIVNKkEEIVGVATFYNRKDGKPF 131
Cdd:smart00065  45 LPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP---LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPF 120
                           90       100
                   ....*....|....*....|....*....
gi 1824718152  132 DEQDEVLMESLTQFLGWSVMNTDTYDKMN 160
Cdd:smart00065 121 TEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
276-361 9.48e-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: 53.84  E-value: 9.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  276 TYHNWRHGFNVAQTMFTLLMTGKLksyytdLEAFAMVTAGLCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 355
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65

                   ....*.
gi 1824718152  356 FLLSEE 361
Cdd:smart00471  66 ILLEEE 71
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
277-462 3.20e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.03  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 277 YHNWRHGFNVAQTMFTLLMTGKLksyyTDLEAFAMVTAGLCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKF 356
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152 357 LLSEETLniyqnlnrrqhEHVIHLMDIAIIATDlALYFKKRAMFQKIVDESKNYQDKkswveylslettrkeivMAMMMT 436
Cdd:cd00077    67 ILRELLL-----------EEVIKLIDELILAVD-ASHHERLDGLGYPDGLKGEEITL-----------------EARIVK 117
                         170       180
                  ....*....|....*....|....*...
gi 1824718152 437 ACDLSAITK--PWEVQSKVALLVAAEFW 462
Cdd:cd00077   118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-150 1.72e-06

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: 47.47  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  53 TPSADHWALASGL------PSYVAESGFICNIMNASADEMFKFQEGALDDSGwlIKNVLSMPIVNKkEEIVGVATFYNRK 126
Cdd:pfam01590  35 LPPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDD-GELLGVLVLHHPR 111
                          90       100
                  ....*....|....*....|....
gi 1824718152 127 DgkPFDEQDEVLMESLTQFLGWSV 150
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
51-165 1.89e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 47.50  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718152  51 IPTPSADHWALASGLPSYVAESGFICNIMNASADEMF-KFQEGALDDSGwlIKNVLSMPIVNKkEEIVGVATFYNRKDGk 129
Cdd:COG2203   248 LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR- 323
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1824718152 130 PFDEQDEVLMESLTQFLGWSVMNTDTYDKMNKLENR 165
Cdd:COG2203   324 AFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
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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