NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767937775|ref|XP_011535956|]
View 

rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha isoform X3 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
199-443 2.95e-108

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 2.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  199 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 277
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  278 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 357
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  358 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 437
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 767937775  438 PMLDGI 443
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
11-82 8.97e-12

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: 62.78  E-value: 8.97e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767937775    11 FQKEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFDEMDETLMESLTQFLGWSVLNPDTYESMN 82
Cdd:smart00065  79 LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
199-443 2.95e-108

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 2.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  199 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 277
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  278 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 357
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  358 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 437
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 767937775  438 PMLDGI 443
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
11-82 8.97e-12

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: 62.78  E-value: 8.97e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767937775    11 FQKEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFDEMDETLMESLTQFLGWSVLNPDTYESMN 82
Cdd:smart00065  79 LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
198-298 2.35e-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: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775   198 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 277
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 767937775   278 TLLRDESLNIFQNLNR---RQHEH 298
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
199-384 1.17e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775 199 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 278
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775 279 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 358
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 767937775 359 ACDLSAITK--PWEVQSQVALLVAAEFW 384
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
2-72 6.11e-04

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: 40.15  E-value: 6.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767937775    2 NAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFDEMDETLMESLTQFLGWSV 72
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
6-87 1.35e-03

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 41.33  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775   6 EDFFAFQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkPFDEMDETLMESLTQFLGWSVLNPDTYESMNKLE 85
Cdd:COG2203  282 PRFAPSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAAL 357

                 ..
gi 767937775  86 NR 87
Cdd:COG2203  358 AA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
199-443 2.95e-108

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 2.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  199 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 277
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  278 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 357
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775  358 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 437
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 767937775  438 PMLDGI 443
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
11-82 8.97e-12

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: 62.78  E-value: 8.97e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767937775    11 FQKEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFDEMDETLMESLTQFLGWSVLNPDTYESMN 82
Cdd:smart00065  79 LFAEDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
198-298 2.35e-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: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775   198 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 277
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 767937775   278 TLLRDESLNIFQNLNR---RQHEH 298
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
199-384 1.17e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775 199 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 278
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775 279 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 358
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 767937775 359 ACDLSAITK--PWEVQSQVALLVAAEFW 384
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
2-72 6.11e-04

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: 40.15  E-value: 6.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767937775    2 NAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFDEMDETLMESLTQFLGWSV 72
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
6-87 1.35e-03

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 41.33  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937775   6 EDFFAFQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkPFDEMDETLMESLTQFLGWSVLNPDTYESMNKLE 85
Cdd:COG2203  282 PRFAPSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAAL 357

                 ..
gi 767937775  86 NR 87
Cdd:COG2203  358 AA 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH