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Conserved domains on  [gi|1958649154|ref|XP_038945075|]
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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A isoform X1 [Rattus norvegicus]

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

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
805-1036 3.06e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 3.06e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  805 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 881
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  882 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 958
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649154  959 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1036
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
558-713 8.48e-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: 8.48e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 636
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154   637 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
356-540 6.19e-10

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.29  E-value: 6.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  356 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 435
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  436 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 510
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958649154  511 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 540
Cdd:COG2203    330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
805-1036 3.06e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 3.06e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  805 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 881
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  882 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 958
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649154  959 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1036
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
558-713 8.48e-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: 8.48e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 636
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154   637 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
558-713 1.27e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 91.41  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:COG2203    208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154  638 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGsAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:COG2203    279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
558-703 4.29e-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: 81.76  E-value: 4.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:pfam01590    2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649154  638 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 703
Cdd:pfam01590   70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
805-978 7.75e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 64.28  E-value: 7.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  805 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 884
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  885 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 962
Cdd:cd00077     69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                          170
                   ....*....|....*.
gi 1958649154  963 WPVTKLTANDIYAEFW 978
Cdd:cd00077    130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
804-963 2.82e-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: 61.93  E-value: 2.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   804 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 883
Cdd:smart00471    2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   884 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlhnqshrdrVIGLMMTACDLCSVTKLW 963
Cdd:smart00471   68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
356-540 6.19e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.29  E-value: 6.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  356 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 435
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  436 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 510
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958649154  511 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 540
Cdd:COG2203    330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
382-525 1.10e-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: 54.79  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  382 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 461
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649154  462 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 525
Cdd:pfam01590   73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
382-527 2.85e-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: 48.15  E-value: 2.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   382 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 461
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   462 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 527
Cdd:smart00065   78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
805-1036 3.06e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 3.06e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  805 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 881
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  882 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 958
Cdd:pfam00233   81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649154  959 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 1036
Cdd:pfam00233  161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
558-713 8.48e-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: 8.48e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 636
Cdd:smart00065    2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154   637 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:smart00065   74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
558-713 1.27e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 91.41  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:COG2203    208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154  638 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGsAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:COG2203    279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
558-703 4.29e-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: 81.76  E-value: 4.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:pfam01590    2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649154  638 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 703
Cdd:pfam01590   70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
559-713 2.11e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 72.62  E-value: 2.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  559 DSLLEHIMIYAKNLVNADRCALFQVDHKNKELYsdLFD-IGEEKEGkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:COG3605     20 DEALDRIVRRIAEALGVDVCSIYLLDPDGGRLE--LRAtEGLNPEA------VGKVRLPLGEGLVGLVAERGEPLNLADA 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649154  638 YADPRFnREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 713
Cdd:COG3605     92 ASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
805-978 7.75e-12

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 64.28  E-value: 7.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  805 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 884
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  885 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 962
Cdd:cd00077     69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                          170
                   ....*....|....*.
gi 1958649154  963 WPVTKLTANDIYAEFW 978
Cdd:cd00077    130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
804-963 2.82e-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: 61.93  E-value: 2.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   804 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 883
Cdd:smart00471    2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   884 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlhnqshrdrVIGLMMTACDLCSVTKLW 963
Cdd:smart00471   68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
356-540 6.19e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.29  E-value: 6.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  356 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 435
Cdd:COG2203    185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  436 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 510
Cdd:COG2203    260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958649154  511 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 540
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 ...
558-704 5.49e-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: 55.55  E-value: 5.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekeGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 637
Cdd:pfam13185    4 LEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW----------GGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649154  638 YADPRFNREVDLYTGYttRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALH 704
Cdd:pfam13185   74 AADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVLALGSN-RPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
382-525 1.10e-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: 54.79  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  382 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 461
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649154  462 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 525
Cdd:pfam01590   73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
382-527 2.85e-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: 48.15  E-value: 2.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   382 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 461
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154   462 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 527
Cdd:smart00065   78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
GAF_3 pfam13492
GAF domain;
558-703 3.41e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 47.36  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  558 IDSLLEHIMIYAKNLVNADRCALFQVDHknkelYSDLFDIGEEKEGKPVFKKTKEIRFSiekgIAGQVARTGEVLNIPDA 637
Cdd:pfam13492    2 LDEILEALLKLLVRLLGAERAAVYLLDE-----DGNKLQVAAGYDGEPDPSESLDADSP----LARRALSSGEPISGLGS 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649154  638 yadprfnrevDLYTGYTTRNILCMPIVSRGSVIGVVqMVNKISGSAFSKTDENNFKMFAVFCALAL 703
Cdd:pfam13492   73 ----------AGEDGLPDGPALVVPLVAGRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAI 127
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
613-672 4.53e-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: 4.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958649154  613 IRFSIEKGIAGQVARTGEVLNIPDAYADPrfnrevdlytGY-----TTRNILCMPIVSRGSVIGV 672
Cdd:COG1956     70 TRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKDGEVIGV 124
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
373-529 2.60e-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: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  373 IEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKE---GQPRLipagPITQGttISAYVAKS 449
Cdd:COG3605      9 ISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPeavGKVRL----PLGEG--LVGLVAER 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649154  450 RKTLLVEDILGDERFPR--GTGLEsgtRIQSVLCLPIVTAiGDLIGILELYRhwgKEAFCLSHQEVAT----ANLawASV 523
Cdd:COG3605     83 GEPLNLADAASHPRFKYfpETGEE---GFRSFLGVPIIRR-GRVLGVLVVQS---REPREFTEEEVEFlvtlAAQ--LAE 153

                   ....*.
gi 1958649154  524 AIHQVQ 529
Cdd:COG3605    154 AIANAE 159
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
435-500 9.13e-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: 37.88  E-value: 9.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649154  435 PITQGttISAYVAKSRKTLLVEDIlgdERFPRGTGLESGTRiqSVLCLPIVtAIGDLIGILELYRH 500
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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