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Conserved domains on  [gi|188595640|ref|NP_001120952|]
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dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A isoform 3 [Rattus norvegicus]

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 1.49e-116

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  413 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188595640  570 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 6.67e-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: 89.75  E-value: 6.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   232 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 188595640   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
53-130 3.74e-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: 3.74e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188595640    53 TKDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASR 130
Cdd:smart00065  75 EADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
413-648 1.49e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  413 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188595640  570 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 6.67e-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: 89.75  E-value: 6.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   232 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 188595640   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
152-308 2.48e-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: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESVEKSsysdwlinNSIAELVAS 231
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188595640  232 TGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 308
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
118-324 4.71e-16

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 82.16  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 118 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 197
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 198 KCSADAENSFKESVEkssysdwlINNSIAELVASTGLPVNVSDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 276
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 188595640 277 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 324
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
53-130 3.74e-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: 3.74e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188595640    53 TKDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASR 130
Cdd:smart00065  75 EADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
413-509 3.08e-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: 58.46  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   413 YHNWRHAFNVCQLMFAMLttagfqEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSalaqlygtsatLEHHHFNHAV 492
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 188595640   493 MILQSEGHNIFANLSSK 509
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
413-589 9.16e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 57.35  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 413 YHNWRHAFNVCQLMFAMlttaGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFqaksdsalaqlYGTSATLEHHHFNHAV 492
Cdd:cd00077    1 EHRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 493 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGAYDWSITSHRDVFRSMLMTACDL--GAV 570
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 188595640 571 TKPWEISRQVAELVTSEFF 589
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-120 8.48e-08

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: 51.71  E-value: 8.48e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188595640   53 TKDRRFNDEIDKLTGYKTKSLLCMPIRNsDGEIIGVAQAINKVPegaPFTEDDEKVMQMYLPFCGIAI 120
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
69-141 6.68e-04

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 6.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188595640  69 KTKSLLCMPIRnSDGEIIGVAQAINKVPEgaPFTEDDEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 141
Cdd:COG3605  107 GFRSFLGVPII-RRGRVLGVLVVQSREPR--EFTEEEVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
413-648 1.49e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 348.77  E-value: 1.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  413 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 492
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  493 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 569
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188595640  570 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 648
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
152-318 6.67e-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: 89.75  E-value: 6.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 231
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   232 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 311
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 188595640   312 IMYDQVK 318
Cdd:smart00065 143 QLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
152-308 2.48e-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: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESVEKSsysdwlinNSIAELVAS 231
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188595640  232 TGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 308
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
118-324 4.71e-16

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 82.16  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 118 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 197
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 198 KCSADAENSFKESVEkssysdwlINNSIAELVASTGLPVNVSDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 276
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 188595640 277 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 324
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
137-329 2.25e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 71.85  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 137 RALLEVVNDLfEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLeDIEspvvkfTKSFELMSpkcsadAENSFKESVEKSSY 216
Cdd:COG3605    4 KALRRISEAV-ASALDLDEALDRIVRRIAEALGVDVCSIYLL-DPD------GGRLELRA------TEGLNPEAVGKVRL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 217 SdwlINNSIAELVASTGLPVNVSDAYQDPRFdAEADQISGFHIRSVLCVPIwNSNHQIIGVAQVLNRlDGKPFDDADQRL 296
Cdd:COG3605   70 P---LGEGLVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPI-IRRGRVLGVLVVQSR-EPREFTEEEVEF 143
                        170       180       190
                 ....*....|....*....|....*....|...
gi 188595640 297 FEAFVIFCGLGINNTIMYDQVKKSWAKQSVALD 329
Cdd:COG3605  144 LVTLAAQLAEAIANAELLGELRAALAELSLARE 176
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
53-130 3.74e-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: 3.74e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188595640    53 TKDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASR 130
Cdd:smart00065  75 EADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
413-509 3.08e-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: 58.46  E-value: 3.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640   413 YHNWRHAFNVCQLMFAMLttagfqEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSalaqlygtsatLEHHHFNHAV 492
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 188595640   493 MILQSEGHNIFANLSSK 509
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
GAF_3 pfam13492
GAF domain;
152-300 6.16e-10

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 57.38  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  152 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmsPKCSADAENSFKESVEkssysdwlINNSIAELVAS 231
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDEDGNKLQ----------VAAGYDGEPDPSESLD--------ADSPLARRALS 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188595640  232 TGLPVNVsdayqdprfdAEADQISGFHIRSVLCVPIwNSNHQIIGVAqVLNRLDGKPFDDADQRLFEAF 300
Cdd:pfam13492  63 SGEPISG----------LGSAGEDGLPDGPALVVPL-VAGRRVIGVL-ALASSKPRAFDAEDLRLLESL 119
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
413-589 9.16e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 57.35  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 413 YHNWRHAFNVCQLMFAMlttaGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFqaksdsalaqlYGTSATLEHHHFNHAV 492
Cdd:cd00077    1 EHRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 493 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGAYDWSITSHRDVFRSMLMTACDL--GAV 570
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 188595640 571 TKPWEISRQVAELVTSEFF 589
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
53-120 8.48e-08

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: 51.71  E-value: 8.48e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188595640   53 TKDRRFNDEIDKLTGYKTKSLLCMPIRNsDGEIIGVAQAINKVPegaPFTEDDEKVMQMYLPFCGIAI 120
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
51-299 4.98e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 49.81  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640  51 TRTKDRRFNDEIDKLTGYKTKSLLCMPIRnSDGEIIGVAQAINKVPegAPFTEDDEKVMQMYLPFCGIAISNAQLFAASR 130
Cdd:COG2203  278 ASTDPRFAPSLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEP--RAFTEEDLELLEALADQAAIAIERARLYEALE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 131 KEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKES 210
Cdd:COG2203  355 AALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLR 434
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 211 VEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFD 290
Cdd:COG2203  435 RILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALL 514

                 ....*....
gi 188595640 291 DADQRLFEA 299
Cdd:COG2203  515 LLLLLLLLL 523
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
229-301 1.87e-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: 42.51  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188595640 229 VASTGLPVNVSDAYQDPRfdaeadqisgfHI------RSVLCVPIWNsNHQIIGV----AQVLNRldgkpFDDADQRLFE 298
Cdd:COG1956   82 AAAEGETQLVPDVHAFPG-----------HIacdsasRSEIVVPIFK-DGEVIGVldidSPTPGR-----FDEEDQAGLE 144

                 ...
gi 188595640 299 AFV 301
Cdd:COG1956  145 ALA 147
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
69-141 6.68e-04

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 6.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188595640  69 KTKSLLCMPIRnSDGEIIGVAQAINKVPEgaPFTEDDEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 141
Cdd:COG3605  107 GFRSFLGVPII-RRGRVLGVLVVQSREPR--EFTEEEVEFLVtlaAQL---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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