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Conserved domains on  [gi|665394063|ref|NP_001287327|]
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phosphodiesterase 6, isoform D [Drosophila melanogaster]

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;
717-950 1.87e-117

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 362.25  E-value: 1.87e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   717 YHNWRHALNVAQTMFAMLKTGKMERFMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESPLAILY-TTSTMEHHHFDQCV 795
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYnDSSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   796 MILNSEGNNIFQALSPEDYRSVMKTVESAILSTDLAMYFKKRNAFLELVENGE---FDWQGEEKKDLLCGMMMTACDVSA 872
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665394063   873 IAKPWEVQHKVAKLVADEFFDQGDLEKlQLNTQPVAMMDRERKDELPKMQVGFIDVICLPLYRVLCDTFPWITPLYEG 950
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQ 237
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
247-406 2.45e-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: 85.90  E-value: 2.45e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    247 DIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRA---SAEEIIIPFGIGIAGMVAQTK 323
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYL--------------VDENDRGELVLVAADGltlPTLGIRFPLDEGLAGRVAETG 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    324 QMINIKEAYKDarFNCEIDLKTGY-KTNAILCMPICNyEGDIIGVAQIINKTNGcMEFDEHDVEIFRRYLTFCGIGIQNA 402
Cdd:smart00065   67 RPLNIPDVEAD--PLFAEDLLGRYqGVRSFLAVPLVA-DGELVGVLALHNKKSP-RPFTEEDEELLQALANQLAIALANA 142

                    ....
gi 665394063    403 QLFE 406
Cdd:smart00065  143 QLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
431-619 3.67e-18

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: 82.43  E-value: 3.67e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    431 NLECLVTKIMTEARELLKCERCSVFLVDldcceashlekiiekPNQPATRAIKSADSFEEKKMRNRFTVLFelggeyqaa 510
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVD---------------ENDRGELVLVAADGLTLPTLGIRFPLDE--------- 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    511 nvsrpsvselssstlaQIAQFVATTGQTVNICDVIEWVRDHNQIraEDEIDSTQAILCMPIMNaQKKVIGVAQLINKANG 590
Cdd:smart00065   57 ----------------GLAGRVAETGRPLNIPDVEADPLFAEDL--LGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSP 117
                           170       180
                    ....*....|....*....|....*....
gi 665394063    591 VPFTDSDASIFEAFAIFCGLGIHNTQMYE 619
Cdd:smart00065  118 RPFTEEDEELLQALANQLAIALANAQLYE 146
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
717-950 1.87e-117

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 362.25  E-value: 1.87e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   717 YHNWRHALNVAQTMFAMLKTGKMERFMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESPLAILY-TTSTMEHHHFDQCV 795
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYnDSSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   796 MILNSEGNNIFQALSPEDYRSVMKTVESAILSTDLAMYFKKRNAFLELVENGE---FDWQGEEKKDLLCGMMMTACDVSA 872
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665394063   873 IAKPWEVQHKVAKLVADEFFDQGDLEKlQLNTQPVAMMDRERKDELPKMQVGFIDVICLPLYRVLCDTFPWITPLYEG 950
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQ 237
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
247-406 2.45e-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: 85.90  E-value: 2.45e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    247 DIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRA---SAEEIIIPFGIGIAGMVAQTK 323
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYL--------------VDENDRGELVLVAADGltlPTLGIRFPLDEGLAGRVAETG 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    324 QMINIKEAYKDarFNCEIDLKTGY-KTNAILCMPICNyEGDIIGVAQIINKTNGcMEFDEHDVEIFRRYLTFCGIGIQNA 402
Cdd:smart00065   67 RPLNIPDVEAD--PLFAEDLLGRYqGVRSFLAVPLVA-DGELVGVLALHNKKSP-RPFTEEDEELLQALANQLAIALANA 142

                    ....
gi 665394063    403 QLFE 406
Cdd:smart00065  143 QLYE 146
GAF COG2203
GAF domain [Signal transduction mechanisms];
223-447 4.77e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.95  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  223 RRHLMDLDEGELFMELIRDVANELDIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRA 302
Cdd:COG2203   183 QRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILL--------------VDEDGGELELVAAPGL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  303 SAEEII-IPFGIGIAGMVAQTKQMINIKEAYKDARF-NCEIDLKTGYKTNAILCMPICnYEGDIIGVAQIINKTNGcmEF 380
Cdd:COG2203   249 PEEELGrLPLGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEPR--AF 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665394063  381 DEHDVEIFRRYLTFCGIGIQNAQLFEMSVQEYRRNQILLNLARSIFEEQNNLECLVTKIMTEARELL 447
Cdd:COG2203   326 TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALL 392
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
431-619 3.67e-18

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: 82.43  E-value: 3.67e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    431 NLECLVTKIMTEARELLKCERCSVFLVDldcceashlekiiekPNQPATRAIKSADSFEEKKMRNRFTVLFelggeyqaa 510
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVD---------------ENDRGELVLVAADGLTLPTLGIRFPLDE--------- 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    511 nvsrpsvselssstlaQIAQFVATTGQTVNICDVIEWVRDHNQIraEDEIDSTQAILCMPIMNaQKKVIGVAQLINKANG 590
Cdd:smart00065   57 ----------------GLAGRVAETGRPLNIPDVEADPLFAEDL--LGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSP 117
                           170       180
                    ....*....|....*....|....*....
gi 665394063    591 VPFTDSDASIFEAFAIFCGLGIHNTQMYE 619
Cdd:smart00065  118 RPFTEEDEELLQALANQLAIALANAQLYE 146
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
717-816 1.67e-14

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: 71.17  E-value: 1.67e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    717 YHNWRHALNVAQTMFAMLKTgkmerfMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESplailyttstMEHHHFDQCVM 796
Cdd:smart00471    3 YHVFEHSLRVAQLAAALAEE------LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV----------LEDHHFIGAEI 66
                            90       100
                    ....*....|....*....|
gi 665394063    797 ILNSEGNNIFQALSPEDYRS 816
Cdd:smart00471   67 LLEEEEPRILEEILRTAILS 86
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
247-399 5.88e-14

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: 69.82  E-value: 5.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   247 DIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRASAEEIIIPFGIGIAgmVAQTKQMI 326
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYL--------------PDADGLEYLPPGARWLKAAGLEIPPGTGVT--VLRTGRPL 64
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665394063   327 NIKEAYKDARFNCEIDLKTGYKTNAILCMPICNyEGDIIGVAQIINKTNgcmEFDEHDVEIFRRYLTFCGIGI 399
Cdd:pfam01590   65 VVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
717-892 1.42e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 69.29  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  717 YHNWRHALNVAQTMFAMLKTGKMerfmTDLEILGLLVACLCHDLDHRGTNNAFqtktesplaiLYTTSTMEHHHFDQCVM 796
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  797 ILNSegnnifqalspEDYRSVMKTVESAILSTDlAMYFKKRNAFlelvenGEFDWQGEEKKDLLCgMMMTACDVSAIAK- 875
Cdd:cd00077    67 ILRE-----------LLLEEVIKLIDELILAVD-ASHHERLDGL------GYPDGLKGEEITLEA-RIVKLADRLDALRr 127
                         170
                  ....*....|....*...
gi 665394063  876 -PWEVQHKVAKLVADEFF 892
Cdd:cd00077   128 dSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
406-684 3.79e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 67.53  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  406 EMSVQEYRRNQILLNLARSIFEEQNnLECLVTKIMTEARELLKCERCSVFLVDldcceashlekiiekpnqPATRAIKSA 485
Cdd:COG2203   183 QRARLELERLALLNEISQALRSALD-LEELLQRILELAGELLGADRGAILLVD------------------EDGGELELV 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  486 dsfeekkmrnrftvlfelggeyQAANVSRPSVSELSSStlAQIAQFVATTGQTVNICDVIEWVRDHNQIRAEDEIDSTQA 565
Cdd:COG2203   244 ----------------------AAPGLPEEELGRLPLG--EGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRS 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  566 ILCMPIMnAQKKVIGVAQLINKANGvPFTDSDASIFEAFAIFCGLGIHNTQMYENACKLMAKQkvALECLSYHATASQDQ 645
Cdd:COG2203   300 LLCVPLL-VDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL--LQELALLRLLLDLEL 375
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 665394063  646 TEKLTQDVIAEAESYNLYSFTFTDFELVDDDTCRAVLRM 684
Cdd:COG2203   376 TLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSG 414
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
431-612 9.01e-11

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: 60.57  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   431 NLECLVTKIMTEARELLKCERCSVFLVDLDCCEAShlekiiekpnqpatraiksadsfeekkmrnrftvlfelggeYQAA 510
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-----------------------------------------PPGA 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   511 NVSRPSVSELSSSTLAQIAQfvatTGQTVNICDVIEwVRDHNQIRAEDEIDSTQAILCMPIMNaQKKVIGVAQLINKANg 590
Cdd:pfam01590   40 RWLKAAGLEIPPGTGVTVLR----TGRPLVVPDAAG-DPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP- 112
                          170       180
                   ....*....|....*....|..
gi 665394063   591 vPFTDSDASIFEAFAIFCGLGI 612
Cdd:pfam01590  113 -PFTEEELELLEVLADQVAIAL 133
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
717-950 1.87e-117

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 362.25  E-value: 1.87e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   717 YHNWRHALNVAQTMFAMLKTGKMERFMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESPLAILY-TTSTMEHHHFDQCV 795
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYnDSSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   796 MILNSEGNNIFQALSPEDYRSVMKTVESAILSTDLAMYFKKRNAFLELVENGE---FDWQGEEKKDLLCGMMMTACDVSA 872
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665394063   873 IAKPWEVQHKVAKLVADEFFDQGDLEKlQLNTQPVAMMDRERKDELPKMQVGFIDVICLPLYRVLCDTFPWITPLYEG 950
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQ 237
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
247-406 2.45e-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: 85.90  E-value: 2.45e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    247 DIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRA---SAEEIIIPFGIGIAGMVAQTK 323
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYL--------------VDENDRGELVLVAADGltlPTLGIRFPLDEGLAGRVAETG 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    324 QMINIKEAYKDarFNCEIDLKTGY-KTNAILCMPICNyEGDIIGVAQIINKTNGcMEFDEHDVEIFRRYLTFCGIGIQNA 402
Cdd:smart00065   67 RPLNIPDVEAD--PLFAEDLLGRYqGVRSFLAVPLVA-DGELVGVLALHNKKSP-RPFTEEDEELLQALANQLAIALANA 142

                    ....
gi 665394063    403 QLFE 406
Cdd:smart00065  143 QLYE 146
GAF COG2203
GAF domain [Signal transduction mechanisms];
223-447 4.77e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.95  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  223 RRHLMDLDEGELFMELIRDVANELDIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRA 302
Cdd:COG2203   183 QRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILL--------------VDEDGGELELVAAPGL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  303 SAEEII-IPFGIGIAGMVAQTKQMINIKEAYKDARF-NCEIDLKTGYKTNAILCMPICnYEGDIIGVAQIINKTNGcmEF 380
Cdd:COG2203   249 PEEELGrLPLGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEPR--AF 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665394063  381 DEHDVEIFRRYLTFCGIGIQNAQLFEMSVQEYRRNQILLNLARSIFEEQNNLECLVTKIMTEARELL 447
Cdd:COG2203   326 TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALL 392
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
431-619 3.67e-18

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: 82.43  E-value: 3.67e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    431 NLECLVTKIMTEARELLKCERCSVFLVDldcceashlekiiekPNQPATRAIKSADSFEEKKMRNRFTVLFelggeyqaa 510
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVD---------------ENDRGELVLVAADGLTLPTLGIRFPLDE--------- 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    511 nvsrpsvselssstlaQIAQFVATTGQTVNICDVIEWVRDHNQIraEDEIDSTQAILCMPIMNaQKKVIGVAQLINKANG 590
Cdd:smart00065   57 ----------------GLAGRVAETGRPLNIPDVEADPLFAEDL--LGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSP 117
                           170       180
                    ....*....|....*....|....*....
gi 665394063    591 VPFTDSDASIFEAFAIFCGLGIHNTQMYE 619
Cdd:smart00065  118 RPFTEEDEELLQALANQLAIALANAQLYE 146
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
717-816 1.67e-14

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: 71.17  E-value: 1.67e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063    717 YHNWRHALNVAQTMFAMLKTgkmerfMTDLEILGLLVACLCHDLDHRGTNNAFQTKTESplailyttstMEHHHFDQCVM 796
Cdd:smart00471    3 YHVFEHSLRVAQLAAALAEE------LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV----------LEDHHFIGAEI 66
                            90       100
                    ....*....|....*....|
gi 665394063    797 ILNSEGNNIFQALSPEDYRS 816
Cdd:smart00471   67 LLEEEEPRILEEILRTAILS 86
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
247-399 5.88e-14

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: 69.82  E-value: 5.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   247 DIDVLCHKILVNVGLLTHADRGSLFLakgtptnkylvaklFDVTQKTALKDAVTRASAEEIIIPFGIGIAgmVAQTKQMI 326
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYL--------------PDADGLEYLPPGARWLKAAGLEIPPGTGVT--VLRTGRPL 64
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665394063   327 NIKEAYKDARFNCEIDLKTGYKTNAILCMPICNyEGDIIGVAQIINKTNgcmEFDEHDVEIFRRYLTFCGIGI 399
Cdd:pfam01590   65 VVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
717-892 1.42e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 69.29  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  717 YHNWRHALNVAQTMFAMLKTGKMerfmTDLEILGLLVACLCHDLDHRGTNNAFqtktesplaiLYTTSTMEHHHFDQCVM 796
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  797 ILNSegnnifqalspEDYRSVMKTVESAILSTDlAMYFKKRNAFlelvenGEFDWQGEEKKDLLCgMMMTACDVSAIAK- 875
Cdd:cd00077    67 ILRE-----------LLLEEVIKLIDELILAVD-ASHHERLDGL------GYPDGLKGEEITLEA-RIVKLADRLDALRr 127
                         170
                  ....*....|....*...
gi 665394063  876 -PWEVQHKVAKLVADEFF 892
Cdd:cd00077   128 dSREKRRRIAEEDLEELL 145
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
237-406 4.10e-13

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 69.15  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  237 ELIRDVANELDIDVLCHKILVNVGLLTHADRGSLFLAKGTPTNKYLVAklfdvTQkTALKDAVTRASaeeiiIPFGIGIA 316
Cdd:COG3605     8 RISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRA-----TE-GLNPEAVGKVR-----LPLGEGLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  317 GMVAQTKQMINIKEAYKDARFNCEIDLK-TGYKtnAILCMPIcNYEGDIIGVAQIINKTNGcmEFDEHDVEIFRRYLTFC 395
Cdd:COG3605    77 GLVAERGEPLNLADAASHPRFKYFPETGeEGFR--SFLGVPI-IRRGRVLGVLVVQSREPR--EFTEEEVEFLVTLAAQL 151
                         170
                  ....*....|.
gi 665394063  396 GIGIQNAQLFE 406
Cdd:COG3605   152 AEAIANAELLG 162
GAF COG2203
GAF domain [Signal transduction mechanisms];
406-684 3.79e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 67.53  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  406 EMSVQEYRRNQILLNLARSIFEEQNnLECLVTKIMTEARELLKCERCSVFLVDldcceashlekiiekpnqPATRAIKSA 485
Cdd:COG2203   183 QRARLELERLALLNEISQALRSALD-LEELLQRILELAGELLGADRGAILLVD------------------EDGGELELV 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  486 dsfeekkmrnrftvlfelggeyQAANVSRPSVSELSSStlAQIAQFVATTGQTVNICDVIEWVRDHNQIRAEDEIDSTQA 565
Cdd:COG2203   244 ----------------------AAPGLPEEELGRLPLG--EGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRS 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  566 ILCMPIMnAQKKVIGVAQLINKANGvPFTDSDASIFEAFAIFCGLGIHNTQMYENACKLMAKQkvALECLSYHATASQDQ 645
Cdd:COG2203   300 LLCVPLL-VDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL--LQELALLRLLLDLEL 375
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 665394063  646 TEKLTQDVIAEAESYNLYSFTFTDFELVDDDTCRAVLRM 684
Cdd:COG2203   376 TLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSG 414
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
431-612 9.01e-11

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: 60.57  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   431 NLECLVTKIMTEARELLKCERCSVFLVDLDCCEAShlekiiekpnqpatraiksadsfeekkmrnrftvlfelggeYQAA 510
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-----------------------------------------PPGA 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   511 NVSRPSVSELSSSTLAQIAQfvatTGQTVNICDVIEwVRDHNQIRAEDEIDSTQAILCMPIMNaQKKVIGVAQLINKANg 590
Cdd:pfam01590   40 RWLKAAGLEIPPGTGVTVLR----TGRPLVVPDAAG-DPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP- 112
                          170       180
                   ....*....|....*....|..
gi 665394063   591 vPFTDSDASIFEAFAIFCGLGI 612
Cdd:pfam01590  113 -PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
431-619 1.39e-07

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 52.98  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  431 NLECLVTKIMTEARELLKCERCSVFLVDLDcceASHLEKIiekpnqpATRAIKSAdsfeekkmrnrftvlfelggeyqAA 510
Cdd:COG3605    18 DLDEALDRIVRRIAEALGVDVCSIYLLDPD---GGRLELR-------ATEGLNPE-----------------------AV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063  511 NVSRPSVSElssstlaQIAQFVATTGQTVNICDViewvRDHNQIRAEDEI--DSTQAILCMPIMnAQKKVIGVAQLINKA 588
Cdd:COG3605    65 GKVRLPLGE-------GLVGLVAERGEPLNLADA----ASHPRFKYFPETgeEGFRSFLGVPII-RRGRVLGVLVVQSRE 132
                         170       180       190
                  ....*....|....*....|....*....|.
gi 665394063  589 NGvPFTDSDASIFEAFAIFCGLGIHNTQMYE 619
Cdd:COG3605   133 PR-EFTEEEVEFLVTLAAQLAEAIANAELLG 162
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
286-400 3.22e-04

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 42.07  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394063   286 LFDVTQKTALKDAVTRASAEEIIIPFGIGIAGMVAQTKQMINIKEAYKDARFNCEIDLKTGYktNAILCMPICnYEGDII 365
Cdd:pfam13185   28 LVDDDGRLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGL--RSFLSVPLV-SGGRVV 104
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 665394063   366 GVAQIINKTNGcmEFDEHDVEIFRRYLTFCGIGIQ 400
Cdd:pfam13185  105 GVLALGSNRPG--AFDEEDLELLELLAEQAAIAIE 137
 
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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