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Conserved domains on  [gi|1958649162|ref|XP_038945099|]
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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A isoform X5 [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;
581-812 7.86e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.56  E-value: 7.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 581 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 657
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 658 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 734
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649162 735 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 812
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
334-489 2.05e-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: 105.54  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 412
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162  413 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
132-316 4.50e-11

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 132 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 211
Cdd:COG2203   185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 212 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 286
Cdd:COG2203   260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958649162 287 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 316
Cdd:COG2203   330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
581-812 7.86e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.56  E-value: 7.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 581 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 657
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 658 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 734
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649162 735 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 812
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
334-489 2.05e-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: 105.54  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 412
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162  413 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
334-489 7.99e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:COG2203   208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162 414 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:COG2203   279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
334-479 1.15e-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: 82.91  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649162 414 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 479
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
581-754 1.34e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 581 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 660
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 661 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 738
Cdd:cd00077    69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                         170
                  ....*....|....*.
gi 1958649162 739 WPVTKLTANDIYAEFW 754
Cdd:cd00077   130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
580-739 1.86e-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: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  580 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 659
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  660 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlhnqshrdrVIGLMMTACDLCSVTKLW 739
Cdd:smart00471  68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
132-316 4.50e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 132 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 211
Cdd:COG2203   185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 212 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 286
Cdd:COG2203   260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958649162 287 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 316
Cdd:COG2203   330 LELLEA-LAdQAAIAIERARLYEALEAALAA 359
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
158-301 3.53e-09

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: 55.95  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 158 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 237
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649162 238 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 301
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
158-303 1.08e-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: 48.92  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  158 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 237
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  238 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 303
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
581-812 7.86e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 312.56  E-value: 7.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 581 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 657
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 658 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 734
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649162 735 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 812
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
334-489 2.05e-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: 105.54  E-value: 2.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 412
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162  413 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
334-489 7.99e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:COG2203   208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162 414 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:COG2203   279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
334-479 1.15e-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: 82.91  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649162 414 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 479
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
335-489 9.61e-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: 9.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 335 DSLLEHIMIYAKNLVNADRCALFQVDHKNKELYsdLFD-IGEEKEGkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:COG3605    20 DEALDRIVRRIAEALGVDVCSIYLLDPDGGRLE--LRAtEGLNPEA------VGKVRLPLGEGLVGLVAERGEPLNLADA 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649162 414 YADPRFnREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 489
Cdd:COG3605    92 ASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
581-754 1.34e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 581 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 660
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 661 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 738
Cdd:cd00077    69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                         170
                  ....*....|....*.
gi 1958649162 739 WPVTKLTANDIYAEFW 754
Cdd:cd00077   130 REKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
580-739 1.86e-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: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  580 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 659
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  660 LQLEGHNIFstlssseyeqvleiirKAIIATDLALYFGNRKQLEEMYQTgslnlhnqshrdrVIGLMMTACDLCSVTKLW 739
Cdd:smart00471  68 LEEEEPRIL----------------EEILRTAILSHHERPDGLRGEPIT-------------LEARIVKVADRLDALRAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
132-316 4.50e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 132 RYQDTNMQGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGp 211
Cdd:COG2203   185 ARLELERLALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 212 itqgTTISAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsH 286
Cdd:COG2203   260 ----EGLAGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----D 329
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958649162 287 QEVATAnLA-WASVAIHQVQVCRGLAKQTEL 316
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 ...
334-480 2.73e-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: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekeGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 413
Cdd:pfam13185   4 LEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW----------GGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649162 414 YADPRFNREVDLYTGYttRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALH 480
Cdd:pfam13185  74 AADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVLALGSN-RPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
158-301 3.53e-09

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: 55.95  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 158 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 237
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649162 238 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 301
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
158-303 1.08e-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: 48.92  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  158 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 237
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162  238 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 303
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
GAF_3 pfam13492
GAF domain;
334-479 2.45e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 47.36  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 334 IDSLLEHIMIYAKNLVNADRCALFQVDHknkelYSDLFDIGEEKEGKPVFKKTKEIRFSiekgIAGQVARTGEVLNIPDA 413
Cdd:pfam13492   2 LDEILEALLKLLVRLLGAERAAVYLLDE-----DGNKLQVAAGYDGEPDPSESLDADSP----LARRALSSGEPISGLGS 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649162 414 yadprfnrevDLYTGYTTRNILCMPIVSRGSVIGVVqMVNKISGSAFSKTDENNFKMFAVFCALAL 479
Cdd:pfam13492  73 ----------AGEDGLPDGPALVVPLVAGRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAI 127
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
389-448 3.50e-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: 3.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958649162 389 IRFSIEKGIAGQVARTGEVLNIPDAYADPrfnrevdlytGY-----TTRNILCMPIVSRGSVIGV 448
Cdd:COG1956    70 TRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKDGEVIGV 124
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
149-305 1.17e-05

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 46.81  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 149 IEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKE---GQPRLipagPITQGttISAYVAKS 225
Cdd:COG3605     9 ISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPeavGKVRL----PLGEG--LVGLVAER 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649162 226 RKTLLVEDILGDERFPR--GTGLEsgtRIQSVLCLPIVTAiGDLIGILELYRhwgKEAFCLSHQEVAT----ANLawASV 299
Cdd:COG3605    83 GEPLNLADAASHPRFKYfpETGEE---GFRSFLGVPIIRR-GRVLGVLVVQS---REPREFTEEEVEFlvtlAAQ--LAE 153

                  ....*.
gi 1958649162 300 AIHQVQ 305
Cdd:COG3605   154 AIANAE 159
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
211-276 7.07e-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: 7.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649162 211 PITQGttISAYVAKSRKTLLVEDIlgdERFPRGTGLESGTRiqSVLCLPIVtAIGDLIGILELYRH 276
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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