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Conserved domains on  [gi|568949996|ref|XP_006507586|]
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cGMP-dependent 3',5'-cyclic phosphodiesterase isoform X1 [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

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
668-901 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.41  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  668 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 747
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  748 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 823
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949996  824 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 901
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
422-571 4.91e-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: 116.33  E-value: 4.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   422 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 498
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949996   499 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 571
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
253-400 3.86e-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: 93.60  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   253 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 330
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949996   331 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 400
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
668-901 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.41  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  668 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 747
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  748 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 823
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949996  824 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 901
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
422-571 4.91e-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: 116.33  E-value: 4.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   422 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 498
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949996   499 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 571
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
253-400 3.86e-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: 93.60  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   253 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 330
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949996   331 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 400
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
668-844 4.34e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 84.70  E-value: 4.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 668 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 747
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 748 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 827
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 568949996 828 --GWKTTRKIAELIYKEFF 844
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
371-582 1.28e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 91.02  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 371 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 450
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 451 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 527
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568949996 528 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 582
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
422-561 3.03e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 76.36  E-value: 3.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  422 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 501
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  502 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 561
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
667-829 2.18e-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: 2.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   667 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 746
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   747 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 826
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 568949996   827 KGW 829
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
147-534 4.01e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.67  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 147 PLARLVAPLAPDMQVLVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDAS 226
Cdd:COG2203   99 LADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 227 EDQKDEKGYTDHDRKILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPL 304
Cdd:COG2203  179 RLLTQRARLELERLALLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 305 TMGRLGQVVEDKQCIQLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfFTDEDEHVIQH 381
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLELLEA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 382 CFHYTGTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGG 461
Cdd:COG2203  336 LADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADL 412
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949996 462 VVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 534
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 ...
251-380 1.82e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 51.31  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  251 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 330
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568949996  331 QLQNMLGCELQAMLCVPVISRatDQVVALACAFNKlGGDFFTDEDEHVIQ 380
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLALGSN-RPGAFDEEDLELLE 126
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
668-901 2.31e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 316.41  E-value: 2.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  668 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 747
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  748 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 823
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949996  824 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 901
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
422-571 4.91e-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: 116.33  E-value: 4.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   422 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 498
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949996   499 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 571
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
253-400 3.86e-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: 93.60  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   253 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 330
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949996   331 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 400
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
668-844 4.34e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 84.70  E-value: 4.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 668 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 747
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 748 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 827
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 568949996 828 --GWKTTRKIAELIYKEFF 844
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
371-582 1.28e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 91.02  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 371 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 450
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 451 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 527
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568949996 528 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 582
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
421-582 3.08e-17

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 80.71  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 421 DDVSVLLQEIITEARNLSNAEICSVFLLDQN----ELVAKVfdgGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 496
Cdd:COG3605   17 LDLDEALDRIVRRIAEALGVDVCSIYLLDPDggrlELRATE---GLNPEAVGKVRLPLGEGLVGLVAERGEPLNLADAAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 497 HPLF-YRGVDDSTGFRTrnILCFPIKNENQeVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 575
Cdd:COG3605   94 HPRFkYFPETGEEGFRS--FLGVPIIRRGR-VLGVLVVQSREPRE-FTEEEVEFLVTLAAQLAEAIANAELLGELRAALA 169

                 ....*..
gi 568949996 576 RSHLANE 582
Cdd:COG3605  170 ELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
422-561 3.03e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 76.36  E-value: 3.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  422 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 501
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  502 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 561
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
667-829 2.18e-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: 2.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   667 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 746
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996   747 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 826
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 568949996   827 KGW 829
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
147-534 4.01e-10

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 63.67  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 147 PLARLVAPLAPDMQVLVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDAS 226
Cdd:COG2203   99 LADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 227 EDQKDEKGYTDHDRKILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPL 304
Cdd:COG2203  179 RLLTQRARLELERLALLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 305 TMGRLGQVVEDKQCIQLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfFTDEDEHVIQH 381
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLELLEA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 382 CFHYTGTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGG 461
Cdd:COG2203  336 LADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADL 412
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949996 462 VVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 534
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 ...
422-562 1.91e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 56.71  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  422 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVAkvFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFY 501
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949996  502 RGVDDSTGFRTrnILCFPIKNENqEVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIA 562
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 ...
251-380 1.82e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 51.31  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  251 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 330
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568949996  331 QLQNMLGCELQAMLCVPVISRatDQVVALACAFNKlGGDFFTDEDEHVIQ 380
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLALGSN-RPGAFDEEDLELLE 126
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
260-380 9.68e-06

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 45.93  E-value: 9.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  260 KVLQYLQQETQATHCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLtMGRLGQVVEDKQCIQLKDLTSDD--VQQLQNMLG 337
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIP-PGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568949996  338 CELQAMLCVPVISRatDQVVALACAFNKlgGDFFTDEDEHVIQ 380
Cdd:pfam01590  85 FGIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
402-548 2.85e-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: 45.20  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996 402 LKCECQALLQVAKNLFTHLDDVSVLLQEiitearNLSNAEICSVFLLD-QNELVAKVFDGGVVddesyEIRIPADQGIAG 480
Cdd:COG1956   12 LLAQLSALLAGETDLIANLANISALLFE------ALPDYNWVGFYLVDgGGELVLGPFQGPPA-----CTRIPFGKGVCG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949996 481 HVATTGQILNIPDAYAHPLFYRgvDDSTgfrTRNILCFPIKNeNQEVIGVAElvnkINGPWFSKFDED 548
Cdd:COG1956   81 TAAAEGETQLVPDVHAFPGHIA--CDSA---SRSEIVVPIFK-DGEVIGVLD----IDSPTPGRFDEE 138
GAF_3 pfam13492
GAF domain;
422-563 4.28e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 43.90  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949996  422 DVSVLLQEIITEARNLSNAEICSVFLLD--QNEL-VAKVFDGGVVDDESyeirIPADQGIAGHVATTGQilnipdayahP 498
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDedGNKLqVAAGYDGEPDPSES----LDADSPLARRALSSGE----------P 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949996  499 LFYRGVDDSTGFRTRNILCFPIKNENQeVIGVaeLVnkINGPWFSKFDED---LATAFSIYCGISIAH 563
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.
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