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Conserved domains on  [gi|578812355|ref|XP_006715384|]
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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A isoform X4 [Homo sapiens]

Protein Classification

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

protein containing domains FhlA, GAF, and HDc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
507-738 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.18  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  507 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 583
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  584 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 660
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578812355  661 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 738
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
260-415 5.18e-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: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 338
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355   339 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
58-242 1.59e-10

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 64.83  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  58 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 137
Cdd:COG2203  185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 138 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 212
Cdd:COG2203  260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                        170       180       190
                 ....*....|....*....|....*....|.
gi 578812355 213 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 242
Cdd:COG2203  330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
507-738 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.18  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  507 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 583
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  584 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 660
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578812355  661 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 738
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
260-415 5.18e-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: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 338
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355   339 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
260-415 6.63e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 6.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:COG2203  208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355 340 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:COG2203  279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
260-405 1.49e-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: 82.53  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812355  340 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 405
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
507-680 1.32e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 507 YHNWKHAVTVAHCMYAILQnnHTLFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 586
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE--ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 587 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTK--L 664
Cdd:cd00077   69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                        170
                 ....*....|....*.
gi 578812355 665 WPVTKLTANDIYAEFW 680
Cdd:cd00077  130 REKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
58-242 1.59e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 64.83  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  58 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 137
Cdd:COG2203  185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 138 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 212
Cdd:COG2203  260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                        170       180       190
                 ....*....|....*....|....*....|.
gi 578812355 213 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 242
Cdd:COG2203  330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
506-665 2.10e-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: 58.85  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   506 PYHNWKHAVTVAHCMYAILQNNHTLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 585
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   586 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlnnqshrdrVIGLMMTACDLCSVTKLW 665
Cdd:smart00471  68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
84-227 1.86e-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: 53.64  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   84 DNQLLLYELSSIIKIATKADGFALYFLGECNNSlciFTPPGIKEGKPRLIPAGPITqgttvSAYVAKSRKTLLVEDILGD 163
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE---YLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578812355  164 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 227
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
84-229 4.77e-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: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355    84 DNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIftpPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD 163
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   164 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 229
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
507-738 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.18  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  507 YHNWKHAVTVAHCMYAILQNN--HTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 583
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGklKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  584 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLNNQSHRDRVIGLMMTACDLCS 660
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578812355  661 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 738
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
260-415 5.18e-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: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 338
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355   339 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
260-415 6.63e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 6.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:COG2203  208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355 340 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:COG2203  279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
260-405 1.49e-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: 82.53  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812355  340 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 405
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
261-415 8.57e-15

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 73.39  E-value: 8.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 261 DSLLEHIMIYAKNLVNADRCALFQVDHKNKELYsdLFD-IGEEKEGkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:COG3605   20 DEALDRIVRRIAEALGVDVCSIYLLDPDGGRLE--LRAtEGLNPEA------VGKVRLPLGEGLVGLVAERGEPLNLADA 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812355 340 YADPRFnREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 415
Cdd:COG3605   92 ASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
507-680 1.32e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 507 YHNWKHAVTVAHCMYAILQnnHTLFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 586
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE--ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 587 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTK--L 664
Cdd:cd00077   69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                        170
                 ....*....|....*.
gi 578812355 665 WPVTKLTANDIYAEFW 680
Cdd:cd00077  130 REKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
58-242 1.59e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 64.83  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  58 RYQDTNMQGVVYELNSYIEQRLDTggdnQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGp 137
Cdd:COG2203  185 ARLELERLALLNEISQALRSALDL----EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 138 itqgTTVSAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 212
Cdd:COG2203  260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                        170       180       190
                 ....*....|....*....|....*....|.
gi 578812355 213 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 242
Cdd:COG2203  330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
506-665 2.10e-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: 58.85  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   506 PYHNWKHAVTVAHCMYAILQNNHTLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 585
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   586 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlnnqshrdrVIGLMMTACDLCSVTKLW 665
Cdd:smart00471  68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
260-406 2.45e-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: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  260 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekeGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 339
Cdd:pfam13185   4 LEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW----------GGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812355  340 YADPRFNREVDLYTGYttRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALH 406
Cdd:pfam13185  74 AADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVLALGSN-RPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
84-227 1.86e-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: 53.64  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   84 DNQLLLYELSSIIKIATKADGFALYFLGECNNSlciFTPPGIKEGKPRLIPAGPITqgttvSAYVAKSRKTLLVEDILGD 163
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE---YLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578812355  164 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 227
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF_3 pfam13492
GAF domain;
260-405 2.20e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 47.36  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  260 IDSLLEHIMIYAKNLVNADRCALFQVDHknkelYSDLFDIGEEKEGKPVFKKTKEIRFSiekgIAGQVARTGEVLNIPDA 339
Cdd:pfam13492   2 LDEILEALLKLLVRLLGAERAAVYLLDE-----DGNKLQVAAGYDGEPDPSESLDADSP----LARRALSSGEPISGLGS 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812355  340 yadprfnrevDLYTGYTTRNILCMPIVSRGSVIGVVqMVNKISGSAFSKTDENNFKMFAVFCALAL 405
Cdd:pfam13492  73 ----------AGEDGLPDGPALVVPLVAGRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAI 127
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
315-374 3.14e-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: 3.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578812355 315 IRFSIEKGIAGQVARTGEVLNIPDAYADPrfnrevdlytGY-----TTRNILCMPIVSRGSVIGV 374
Cdd:COG1956   70 TRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKDGEVIGV 124
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
84-229 4.77e-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: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355    84 DNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIftpPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD 163
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355   164 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 229
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
75-231 1.34e-05

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 46.43  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355  75 IEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKE---GKPRLipagPITQGttVSAYVAKS 151
Cdd:COG3605    9 ISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPeavGKVRL----PLGEG--LVGLVAER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812355 152 RKTLLVEDILGDERFPR--GTGLEsgtRIQSVLCLPIVTAiGDLIGILELYRhwgKEAFCLSHQEVAT----ANLawASV 225
Cdd:COG3605   83 GEPLNLADAASHPRFKYfpETGEE---GFRSFLGVPIIRR-GRVLGVLVVQS---REPREFTEEEVEFlvtlAAQ--LAE 153

                 ....*.
gi 578812355 226 AIHQVQ 231
Cdd:COG3605  154 AIANAE 159
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
137-202 2.87e-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: 2.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812355 137 PITQGttVSAYVAKSRKTLLVEDIlgdERFPRGTGLESGTRiqSVLCLPIVtAIGDLIGILELYRH 202
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.
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