NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1866609487|ref|NP_001372008|]
View 

cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A isoform 3 [Homo sapiens]

Protein Classification

GAF and HDc domain-containing protein( domain architecture ID 10789072)

protein containing domains FhlA, GAF, and HDc

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
790-1021 3.45e-102

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 320.65  E-value: 3.45e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  790 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 866
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  867 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 943
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1866609487  944 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1021
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
543-698 7.04e-26

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: 104.39  E-value: 7.04e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 621
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487   622 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
341-525 5.22e-10

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.67  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  341 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 420
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  421 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 495
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1866609487  496 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 525
Cdd:COG2203    330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
790-1021 3.45e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 320.65  E-value: 3.45e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  790 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 866
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  867 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 943
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1866609487  944 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1021
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
543-698 7.04e-26

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: 104.39  E-value: 7.04e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 621
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487   622 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
543-698 2.43e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 93.72  E-value: 2.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:COG2203    208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487  623 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGsAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:COG2203    279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
543-688 2.88e-18

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: 82.14  E-value: 2.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:pfam01590    2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1866609487  623 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 688
Cdd:pfam01590   70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
790-963 1.64e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 66.21  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  790 YHNWKHAVTVAHCMYAILQnnHTLFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 869
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAE--ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  870 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTK--L 947
Cdd:cd00077     69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                          170
                   ....*....|....*.
gi 1866609487  948 WPVTKLTANDIYAEFW 963
Cdd:cd00077    130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
789-948 6.69e-11

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: 60.77  E-value: 6.69e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   789 PYHNWKHAVTVAHCMYAILQNNHTLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 868
Cdd:smart00471    2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   869 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlnnqshrdrVIGLMMTACDLCSVTKLW 948
Cdd:smart00471   68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
341-525 5.22e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.67  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  341 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 420
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  421 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 495
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1866609487  496 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 525
Cdd:COG2203    330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
367-510 3.20e-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: 53.25  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  367 DNQLLLYELSSIIKIATKADGFALYFLGECNNSlciFTPPGIKEGKPRLIPAGPITqgttvSAYVAKSRKTLLVEDILGD 446
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLE---YLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1866609487  447 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 510
Cdd:pfam01590   73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
367-512 6.41e-06

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: 46.99  E-value: 6.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   367 DNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIftpPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD 446
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   447 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 512
Cdd:smart00065   78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
790-1021 3.45e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 320.65  E-value: 3.45e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  790 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 866
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  867 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 943
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1866609487  944 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1021
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
543-698 7.04e-26

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: 104.39  E-value: 7.04e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 621
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487   622 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
543-698 2.43e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 93.72  E-value: 2.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:COG2203    208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487  623 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGsAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:COG2203    279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
543-688 2.88e-18

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: 82.14  E-value: 2.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:pfam01590    2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1866609487  623 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 688
Cdd:pfam01590   70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
544-698 1.55e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 73.01  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  544 DSLLEHIMIYAKNLVNADRCALFQVDHKNKELYsdLFD-IGEEKEGkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:COG3605     20 DEALDRIVRRIAEALGVDVCSIYLLDPDGGRLE--LRAtEGLNPEA------VGKVRLPLGEGLVGLVAERGEPLNLADA 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1866609487  623 YADPRFnREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 698
Cdd:COG3605     92 ASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
790-963 1.64e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 66.21  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  790 YHNWKHAVTVAHCMYAILQnnHTLFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 869
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAE--ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  870 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTK--L 947
Cdd:cd00077     69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                          170
                   ....*....|....*.
gi 1866609487  948 WPVTKLTANDIYAEFW 963
Cdd:cd00077    130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
789-948 6.69e-11

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: 60.77  E-value: 6.69e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   789 PYHNWKHAVTVAHCMYAILQNNHTLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 868
Cdd:smart00471    2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   869 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlnnqshrdrVIGLMMTACDLCSVTKLW 948
Cdd:smart00471   68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
341-525 5.22e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.67  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  341 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 420
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  421 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 495
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1866609487  496 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 525
Cdd:COG2203    330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
543-689 3.45e-09

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: 56.32  E-value: 3.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekeGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 622
Cdd:pfam13185    4 LEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW----------GGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1866609487  623 YADPRFNREVDLYTGYttRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALH 689
Cdd:pfam13185   74 AADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVLALGSN-RPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
367-510 3.20e-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: 53.25  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  367 DNQLLLYELSSIIKIATKADGFALYFLGECNNSlciFTPPGIKEGKPRLIPAGPITqgttvSAYVAKSRKTLLVEDILGD 446
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLE---YLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1866609487  447 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 510
Cdd:pfam01590   73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF_3 pfam13492
GAF domain;
543-688 3.09e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 47.36  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  543 IDSLLEHIMIYAKNLVNADRCALFQVDHknkelYSDLFDIGEEKEGKPVFKKTKEIRFSiekgIAGQVARTGEVLNIPDA 622
Cdd:pfam13492    2 LDEILEALLKLLVRLLGAERAAVYLLDE-----DGNKLQVAAGYDGEPDPSESLDADSP----LARRALSSGEPISGLGS 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1866609487  623 yadprfnrevDLYTGYTTRNILCMPIVSRGSVIGVVqMVNKISGSAFSKTDENNFKMFAVFCALAL 688
Cdd:pfam13492   73 ----------AGEDGLPDGPALVVPLVAGRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAI 127
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
598-657 4.44e-06

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 47.51  E-value: 4.44e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1866609487  598 IRFSIEKGIAGQVARTGEVLNIPDAYADPrfnrevdlytGY-----TTRNILCMPIVSRGSVIGV 657
Cdd:COG1956     70 TRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKDGEVIGV 124
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
367-512 6.41e-06

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: 46.99  E-value: 6.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   367 DNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIftpPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD 446
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487   447 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 512
Cdd:smart00065   78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
358-514 2.55e-05

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 46.04  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  358 IEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKE---GKPRLipagPITQGttVSAYVAKS 434
Cdd:COG3605      9 ISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPeavGKVRL----PLGEG--LVGLVAER 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1866609487  435 RKTLLVEDILGDERFPR--GTGLEsgtRIQSVLCLPIVTAiGDLIGILELYRhwgKEAFCLSHQEVAT----ANLawASV 508
Cdd:COG3605     83 GEPLNLADAASHPRFKYfpETGEE---GFRSFLGVPIIRR-GRVLGVLVVQS---REPREFTEEEVEFlvtlAAQ--LAE 153

                   ....*.
gi 1866609487  509 AIHQVQ 514
Cdd:COG3605    154 AIANAE 159
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
420-485 4.05e-03

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 39.04  E-value: 4.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1866609487  420 PITQGttVSAYVAKSRKTLLVEDIlgdERFPRGTGLESGTRiqSVLCLPIVtAIGDLIGILELYRH 485
Cdd:COG1956     73 PFGKG--VCGTAAAEGETQLVPDV---HAFPGHIACDSASR--SEIVVPIF-KDGEVIGVLDIDSP 130
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH