NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|344217719|ref|NP_001230687|]
View 

cGMP-dependent 3',5'-cyclic phosphodiesterase isoform 5 [Mus musculus]

Protein Classification

3',5'-cyclic nucleotide phosphodiesterase( domain architecture ID 10637639)

3',5'-cyclic nucleotide phosphodiesterase catalyzes the hydrolysis of cAMP or cGMP to produce adenosine 5'-phosphate or guanosine 5'-phosphate, respectively

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
660-893 2.46e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.03  E-value: 2.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  660 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 739
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  740 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 815
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344217719  816 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 893
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
414-563 6.51e-30

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: 115.94  E-value: 6.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   414 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 490
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719   491 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 563
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
245-392 5.16e-22

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: 93.21  E-value: 5.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   245 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 322
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344217719   323 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 392
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
660-893 2.46e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.03  E-value: 2.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  660 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 739
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  740 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 815
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344217719  816 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 893
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
414-563 6.51e-30

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: 115.94  E-value: 6.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   414 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 490
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719   491 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 563
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
245-392 5.16e-22

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: 93.21  E-value: 5.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   245 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 322
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344217719   323 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 392
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
660-836 3.69e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.08  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 660 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 739
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 740 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 819
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 344217719 820 --GWKTTRKIAELIYKEFF 836
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
363-574 4.38e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.48  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 363 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 442
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 443 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 519
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 344217719 520 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 574
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
414-553 4.34e-16

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: 75.59  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  414 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 493
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  494 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 553
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
659-821 1.86e-14

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: 70.79  E-value: 1.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   659 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 738
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   739 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 818
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 344217719   819 KGW 821
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
139-526 1.02e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 62.52  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 139 PLARLVAPLAPDMQVLVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDAS 218
Cdd:COG2203   99 LADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 219 EDQKDEKGYTDHDRKILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPL 296
Cdd:COG2203  179 RLLTQRARLELERLALLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 297 TMGRLGQVVEDKQCIQLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfFTDEDEHVIQH 373
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLELLEA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 374 CFHYTGTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGG 453
Cdd:COG2203  336 LADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADL 412
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719 454 VVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 526
Cdd:COG2203  413 SGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
243-372 2.44e-07

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: 50.93  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  243 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 322
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 344217719  323 QLQNMLGCELQAMLCVPVISRatDQVVALACAFNKlGGDFFTDEDEHVIQ 372
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLALGSN-RPGAFDEEDLELLE 126
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
660-893 2.46e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.03  E-value: 2.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  660 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 739
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  740 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 815
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344217719  816 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 893
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
414-563 6.51e-30

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: 115.94  E-value: 6.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   414 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 490
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719   491 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 563
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
245-392 5.16e-22

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: 93.21  E-value: 5.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   245 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 322
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344217719   323 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 392
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
660-836 3.69e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.08  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 660 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 739
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 740 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 819
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 344217719 820 --GWKTTRKIAELIYKEFF 836
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
363-574 4.38e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.48  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 363 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 442
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 443 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 519
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 344217719 520 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 574
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
413-574 3.88e-17

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 80.33  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 413 DDVSVLLQEIITEARNLSNAEICSVFLLDQN----ELVAKVfdgGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 488
Cdd:COG3605   17 LDLDEALDRIVRRIAEALGVDVCSIYLLDPDggrlELRATE---GLNPEAVGKVRLPLGEGLVGLVAERGEPLNLADAAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 489 HPLF-YRGVDDSTGFRTrnILCFPIKNENQeVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 567
Cdd:COG3605   94 HPRFkYFPETGEEGFRS--FLGVPIIRRGR-VLGVLVVQSREPRE-FTEEEVEFLVTLAAQLAEAIANAELLGELRAALA 169

                 ....*..
gi 344217719 568 RSHLANE 574
Cdd:COG3605  170 ELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
414-553 4.34e-16

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: 75.59  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  414 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 493
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  494 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 553
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
659-821 1.86e-14

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: 70.79  E-value: 1.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   659 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 738
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719   739 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 818
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 344217719   819 KGW 821
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
139-526 1.02e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 62.52  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 139 PLARLVAPLAPDMQVLVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDAS 218
Cdd:COG2203   99 LADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 219 EDQKDEKGYTDHDRKILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPL 296
Cdd:COG2203  179 RLLTQRARLELERLALLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 297 TMGRLGQVVEDKQCIQLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfFTDEDEHVIQH 373
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLELLEA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 374 CFHYTGTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGG 453
Cdd:COG2203  336 LADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADL 412
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719 454 VVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 526
Cdd:COG2203  413 SGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
414-554 2.50e-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: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  414 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVAkvFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFY 493
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344217719  494 RGVDDSTGFRTrnILCFPIKNENqEVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIA 554
Cdd:pfam13185  81 GLPAGHAGLRS--FLSVPLVSGG-RVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
243-372 2.44e-07

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: 50.93  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  243 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 322
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 344217719  323 QLQNMLGCELQAMLCVPVISRatDQVVALACAFNKlGGDFFTDEDEHVIQ 372
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLALGSN-RPGAFDEEDLELLE 126
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
252-372 1.19e-05

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: 45.93  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  252 KVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPltmGRLGQVVEDKQCIQLKDLTSDD--VQQLQNMLG 329
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP---GTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 344217719  330 CELQAMLCVPVISRatDQVVALACAFNKlgGDFFTDEDEHVIQ 372
Cdd:pfam01590  85 FGIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
389-540 3.29e-05

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


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 44.82  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719 389 QKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEiitearNLSNAEICSVFLLD-QNELVAKVFDGGVVddesyEIRIPAD 467
Cdd:COG1956    7 EDYDELLAQLSALLAGETDLIANLANISALLFE------ALPDYNWVGFYLVDgGGELVLGPFQGPPA-----CTRIPFG 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344217719 468 QGIAGHVATTGQILNIPDAYAHPLFYRgvDDSTgfrTRNILCFPIKNeNQEVIGVAElvnkINGPWFSKFDED 540
Cdd:COG1956   76 KGVCGTAAAEGETQLVPDVHAFPGHIA--CDSA---SRSEIVVPIFK-DGEVIGVLD----IDSPTPGRFDEE 138
GAF_3 pfam13492
GAF domain;
414-555 7.71e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 43.51  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344217719  414 DVSVLLQEIITEARNLSNAEICSVFLLD--QNEL-VAKVFDGGVVDDESyeirIPADQGIAGHVATTGQilnipdayahP 490
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDedGNKLqVAAGYDGEPDPSES----LDADSPLARRALSSGE----------P 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344217719  491 LFYRGVDDSTGFRTRNILCFPIKNENQeVIGVaeLVnkINGPWFSKFDED---LATAFSIYCGISIAH 555
Cdd:pfam13492  67 ISGLGSAGEDGLPDGPALVVPLVAGRR-VIGV--LA--LASSKPRAFDAEdlrLLESLAAQIATAIEN 129
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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