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Conserved domains on  [gi|116536087|ref|NP_001070665|]
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dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A 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;
413-648 1.60e-116

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.60e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  413 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116536087  570 VTKPWEISRQVAELVTSEFFEQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 2.78e-21

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: 90.52  E-value: 2.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   232 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 116536087   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
40-130 3.23e-11

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: 61.63  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087    40 EKHQDFLIQRQTKtkDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIA 119
Cdd:smart00065  64 ETGRPLNIPDVEA--DPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIA 138
                           90
                   ....*....|.
gi 116536087   120 ISNAQLFAASR 130
Cdd:smart00065 139 LANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
413-648 1.60e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.60e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  413 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116536087  570 VTKPWEISRQVAELVTSEFFEQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 2.78e-21

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: 90.52  E-value: 2.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   232 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 116536087   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
118-324 5.24e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 85.25  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 118 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 197
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 198 KCSADAENSFKESMEkssysdwlINNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 276
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 116536087 277 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 324
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
152-308 2.20e-16

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: 75.98  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESMEKSsysdwlinNSIAELVAS 231
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116536087  232 TGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 308
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
40-130 3.23e-11

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: 61.63  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087    40 EKHQDFLIQRQTKtkDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIA 119
Cdd:smart00065  64 ETGRPLNIPDVEA--DPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIA 138
                           90
                   ....*....|.
gi 116536087   120 ISNAQLFAASR 130
Cdd:smart00065 139 LANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
413-589 3.59e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.89  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 413 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 492
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 493 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGEYDWNIKNHRDIFRSMLMTACDL--GAV 570
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 116536087 571 TKPWEISRQVAELVTSEFF 589
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
413-509 4.23e-10

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: 58.08  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   413 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 492
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 116536087   493 MILQSEGHNIFANLSSK 509
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-120 1.11e-07

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: 51.33  E-value: 1.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116536087   53 TKDRRFNDEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKIPegaPFTEDDEKVMQMYLPFCGIAI 120
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
69-141 1.70e-03

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116536087  69 KTKSLLCMPIRSsDGEIIGVAQAINKipEGAPFTEDDEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 141
Cdd:COG3605  107 GFRSFLGVPIIR-RGRVLGVLVVQSR--EPREFTEEEVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
413-648 1.60e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.60e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  413 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116536087  570 VTKPWEISRQVAELVTSEFFEQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 2.78e-21

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: 90.52  E-value: 2.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   232 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 116536087   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
118-324 5.24e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 85.25  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 118 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 197
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 198 KCSADAENSFKESMEkssysdwlINNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 276
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 116536087 277 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 324
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
152-308 2.20e-16

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: 75.98  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESMEKSsysdwlinNSIAELVAS 231
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116536087  232 TGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 308
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
137-329 7.71e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 70.31  E-value: 7.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 137 RALLEVVNDLfEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLeDIEspvvkfTKSFELMSpkcsadAENSFKESMEKSSY 216
Cdd:COG3605    4 KALRRISEAV-ASALDLDEALDRIVRRIAEALGVDVCSIYLL-DPD------GGRLELRA------TEGLNPEAVGKVRL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 217 SdwlINNSIAELVASTGLPVNISDAYQDPRFdAEADQISGFHIRSVLCVPIwNSNHQIIGVAQVLNRlDGKPFDDADQRL 296
Cdd:COG3605   70 P---LGEGLVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPI-IRRGRVLGVLVVQSR-EPREFTEEEVEF 143
                        170       180       190
                 ....*....|....*....|....*....|...
gi 116536087 297 FEAFVIFCGLGINNTIMYDQVKKSWAKQSVALD 329
Cdd:COG3605  144 LVTLAAQLAEAIANAELLGELRAALAELSLARE 176
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
40-130 3.23e-11

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: 61.63  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087    40 EKHQDFLIQRQTKtkDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIA 119
Cdd:smart00065  64 ETGRPLNIPDVEA--DPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIA 138
                           90
                   ....*....|.
gi 116536087   120 ISNAQLFAASR 130
Cdd:smart00065 139 LANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
413-589 3.59e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.89  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 413 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 492
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 493 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGEYDWNIKNHRDIFRSMLMTACDL--GAV 570
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 116536087 571 TKPWEISRQVAELVTSEFF 589
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
413-509 4.23e-10

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: 58.08  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087   413 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 492
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 116536087   493 MILQSEGHNIFANLSSK 509
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
GAF_3 pfam13492
GAF domain;
152-300 4.55e-10

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 57.77  E-value: 4.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmsPKCSADAENSFKESMEkssysdwlINNSIAELVAS 231
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDEDGNKLQ----------VAAGYDGEPDPSESLD--------ADSPLARRALS 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116536087  232 TGLPVnisdayqdprFDAEADQISGFHIRSVLCVPIwNSNHQIIGVAqVLNRLDGKPFDDADQRLFEAF 300
Cdd:pfam13492  63 SGEPI----------SGLGSAGEDGLPDGPALVVPL-VAGRRVIGVL-ALASSKPRAFDAEDLRLLESL 119
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-120 1.11e-07

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: 51.33  E-value: 1.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116536087   53 TKDRRFNDEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKIPegaPFTEDDEKVMQMYLPFCGIAI 120
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
53-299 3.94e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.19  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087  53 TKDRRFND-EIDKLTGYKTKSLLCMPIRSsDGEIIGVAQAINKipEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASRK 131
Cdd:COG2203  279 STDPRFAPsLRELLLALGIRSLLCVPLLV-DGRLIGVLALYSK--EPRAFTEEDLELLEALADQAAIAIERARLYEALEA 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 132 EYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESM 211
Cdd:COG2203  356 ALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRR 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 212 EKSSYSDWLINNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDD 291
Cdd:COG2203  436 ILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLL 515

                 ....*...
gi 116536087 292 ADQRLFEA 299
Cdd:COG2203  516 LLLLLLLL 523
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
229-301 5.01e-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: 40.97  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116536087 229 VASTGLPVNISDAYQDPRfdaeadqisgfHI------RSVLCVPIWNsNHQIIGV----AQVLNRldgkpFDDADQRLFE 298
Cdd:COG1956   82 AAAEGETQLVPDVHAFPG-----------HIacdsasRSEIVVPIFK-DGEVIGVldidSPTPGR-----FDEEDQAGLE 144

                 ...
gi 116536087 299 AFV 301
Cdd:COG1956  145 ALA 147
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
69-141 1.70e-03

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116536087  69 KTKSLLCMPIRSsDGEIIGVAQAINKipEGAPFTEDDEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 141
Cdd:COG3605  107 GFRSFLGVPIIR-RGRVLGVLVVQSR--EPREFTEEEVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
 
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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