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Conserved domains on  [gi|1958649166|ref|XP_038945109|]
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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A isoform X7 [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;
444-675 2.27e-100

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 307.94  E-value: 2.27e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 444 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 520
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 521 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 597
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649166 598 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 675
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
197-352 6.13e-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: 104.00  E-value: 6.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 275
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166  276 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-179 5.63e-11

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 65.99  E-value: 5.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166   2 QGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGpitqgTTI 81
Cdd:COG2203   192 LALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG-----EGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  82 SAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsHQEVATAn 156
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----DLELLEA- 335
                         170       180
                  ....*....|....*....|....
gi 1958649166 157 LA-WASVAIHQVQVCRGLAKQTEL 179
Cdd:COG2203   336 LAdQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
444-675 2.27e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 307.94  E-value: 2.27e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 444 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 520
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 521 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 597
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649166 598 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 675
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
197-352 6.13e-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: 104.00  E-value: 6.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 275
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166  276 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
197-352 5.64e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 5.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:COG2203   208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166 277 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:COG2203   279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
197-342 1.97e-18

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 82.14  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649166 277 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 342
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
444-617 5.28e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 61.20  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 444 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 523
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 524 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 601
Cdd:cd00077    69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                         170
                  ....*....|....*.
gi 1958649166 602 WPVTKLTANDIYAEFW 617
Cdd:cd00077   130 REKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-179 5.63e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 65.99  E-value: 5.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166   2 QGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGpitqgTTI 81
Cdd:COG2203   192 LALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG-----EGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  82 SAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsHQEVATAn 156
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----DLELLEA- 335
                         170       180
                  ....*....|....*....|....
gi 1958649166 157 LA-WASVAIHQVQVCRGLAKQTEL 179
Cdd:COG2203   336 LAdQAAIAIERARLYEALEAALAA 359
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
443-531 6.77e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 60.39  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  443 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 522
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67

                   ....*....
gi 1958649166  523 LQLEGHNIF 531
Cdd:smart00471  68 LEEEEPRIL 76
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
21-164 5.14e-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: 55.18  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  21 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 100
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649166 101 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 164
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
21-166 1.96e-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: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166   21 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 100
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  101 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 166
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
444-675 2.27e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 307.94  E-value: 2.27e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 444 YHNWKHAVTVAHCMYAILQNNN--GLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYST-STMEQHHFSQTV 520
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKlkEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 521 SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSL---NLHNQSHRDRVIGLMMTACDLCS 597
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649166 598 VTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKAC 675
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
197-352 6.13e-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: 104.00  E-value: 6.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNK-ELYSDLFDIGEEKegkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPD 275
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLP--------TLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166  276 AYADPRFNREVDLYTGYTtRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:smart00065  74 VEADPLFAEDLLGRYQGV-RSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
197-352 5.64e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 94.88  E-value: 5.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELysdlfdigeEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:COG2203   208 LEELLQRILELAGELLGADRGAILLVDEDGGEL---------ELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVNDA 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166 277 YADPRF-NREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:COG2203   279 STDPRFaPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARLYEALE 354
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
197-342 1.97e-18

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 82.14  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekegkPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPDADGLEYLP------------PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649166 277 YADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKisGSAFSKTDENNFKMFAVFCALAL 342
Cdd:pfam01590  70 AGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
198-352 7.81e-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: 7.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 198 DSLLEHIMIYAKNLVNADRCALFQVDHKNKELYsdLFD-IGEEKEGkpvfkkTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:COG3605    20 DEALDRIVRRIAEALGVDVCSIYLLDPDGGRLE--LRAtEGLNPEA------VGKVRLPLGEGLVGLVAERGEPLNLADA 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649166 277 YADPRFnREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALHCANMYHRIR 352
Cdd:COG3605    92 ASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
444-617 5.28e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 61.20  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 444 YHNWKHAVTVAHCMYAILQNNNglFTDLERKGLLIACLCHDLDHRGFSNSYlqkfdhplaaLYSTSTMEQHHFSQTVSIL 523
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG--LSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAEIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 524 QleghnifstlsSSEYEQVLEIIRKAIIATDlalyfgnrKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTK--L 601
Cdd:cd00077    69 R-----------ELLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdS 129
                         170
                  ....*....|....*.
gi 1958649166 602 WPVTKLTANDIYAEFW 617
Cdd:cd00077   130 REKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-179 5.63e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 65.99  E-value: 5.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166   2 QGVVYELNSYIEQRLDTGGdnhlLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGpitqgTTI 81
Cdd:COG2203   192 LALLNEISQALRSALDLEE----LLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLG-----EGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  82 SAYVAKSRKTLLVEDILGDERFPRGT-GLESGTRIQSVLCLPIVTAiGDLIGILELY----RHWGKEafclsHQEVATAn 156
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFAPSLrELLLALGIRSLLCVPLLVD-GRLIGVLALYskepRAFTEE-----DLELLEA- 335
                         170       180
                  ....*....|....*....|....
gi 1958649166 157 LA-WASVAIHQVQVCRGLAKQTEL 179
Cdd:COG2203   336 LAdQAAIAIERARLYEALEAALAA 359
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
443-531 6.77e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 60.39  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  443 PYHNWKHAVTVAHCMYAILQNNNGLFTDLerkgLLIACLCHDLDHRGFSNSYLQKfdhplaalysTSTMEQHHFSQTVSI 522
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLDIEL----LLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEIL 67

                   ....*....
gi 1958649166  523 LQLEGHNIF 531
Cdd:smart00471  68 LEEEEPRIL 76
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
197-343 2.25e-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: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSdlfdigeekeGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDA 276
Cdd:pfam13185   4 LEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW----------GGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649166 277 YADPRFNREVDLYTGYttRNILCMPIVSRGSVIGVVQMVNKiSGSAFSKTDENNFKMFAVFCALALH 343
Cdd:pfam13185  74 AADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVLALGSN-RPGAFDEEDLELLELLAEQAAIAIE 137
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
21-164 5.14e-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: 55.18  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  21 DNHLLLYELSSIIRIATKADGFALYFLGECNnslCVFTPPGMKEGQPRLIPAGPITqgttiSAYVAKSRKTLLVEDILGD 100
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG---LEYLPPGARWLKAAGLEIPPGT-----GVTVLRTGRPLVVPDAAGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649166 101 ERFPRGTGLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEVATANLAWASVAI 164
Cdd:pfam01590  73 PRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
21-166 1.96e-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: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166   21 DNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVftpPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD 100
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELV---LVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEAD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  101 ERFPRGTgLESGTRIQSVLCLPIVTAiGDLIGILELYRHwgKEAFCLSHQEV----ATANLAWASVAIHQ 166
Cdd:smart00065  78 PLFAEDL-LGRYQGVRSFLAVPLVAD-GELVGVLALHNK--KSPRPFTEEDEellqALANQLAIALANAQ 143
GAF_3 pfam13492
GAF domain;
197-342 2.02e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 47.36  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166 197 IDSLLEHIMIYAKNLVNADRCALFQVDHknkelYSDLFDIGEEKEGKPVFKKTKEIRFSiekgIAGQVARTGEVLNIPDA 276
Cdd:pfam13492   2 LDEILEALLKLLVRLLGAERAAVYLLDE-----DGNKLQVAAGYDGEPDPSESLDADSP----LARRALSSGEPISGLGS 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649166 277 yadprfnrevDLYTGYTTRNILCMPIVSRGSVIGVVqMVNKISGSAFSKTDENNFKMFAVFCALAL 342
Cdd:pfam13492  73 ----------AGEDGLPDGPALVVPLVAGRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAI 127
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
252-311 2.87e-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: 2.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958649166 252 IRFSIEKGIAGQVARTGEVLNIPDAYADPrfnrevdlytGY-----TTRNILCMPIVSRGSVIGV 311
Cdd:COG1956    70 TRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKDGEVIGV 124
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
12-168 9.56e-06

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: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  12 IEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKE---GQPRLipagPITQGttISAYVAKS 88
Cdd:COG3605     9 ISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPeavGKVRL----PLGEG--LVGLVAER 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649166  89 RKTLLVEDILGDERFPR--GTGLEsgtRIQSVLCLPIVTAiGDLIGILELYRhwgKEAFCLSHQEVAT----ANLawASV 162
Cdd:COG3605    83 GEPLNLADAASHPRFKYfpETGEE---GFRSFLGVPIIRR-GRVLGVLVVQS---REPREFTEEEVEFlvtlAAQ--LAE 153

                  ....*.
gi 1958649166 163 AIHQVQ 168
Cdd:COG3605   154 AIANAE 159
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
74-139 5.81e-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: 5.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649166  74 PITQGttISAYVAKSRKTLLVEDIlgdERFPRGTGLESGTRiqSVLCLPIVtAIGDLIGILELYRH 139
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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