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Conserved domains on  [gi|568950008|ref|XP_006507592|]
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cGMP-dependent 3',5'-cyclic phosphodiesterase isoform X6 [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;
514-747 1.17e-100

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 311.02  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  514 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 593
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  594 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 669
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950008  670 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 747
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
268-417 4.06e-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: 4.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   268 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 344
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568950008   345 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 417
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
95-246 3.39e-20

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: 87.82  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008    95 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 172
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568950008   173 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFptssFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 246
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRP----FTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
514-747 1.17e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 311.02  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  514 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 593
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  594 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 669
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950008  670 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 747
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
268-417 4.06e-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: 4.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   268 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 344
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568950008   345 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 417
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
95-246 3.39e-20

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: 87.82  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008    95 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 172
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568950008   173 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFptssFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 246
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRP----FTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
217-428 3.40e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.56  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 217 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 296
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 297 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 373
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568950008 374 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 428
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
514-690 8.05e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 83.93  E-value: 8.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 514 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 593
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 594 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 673
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 568950008 674 --GWKTTRKIAELIYKEFF 690
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
268-407 1.87e-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: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  268 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 347
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  348 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 407
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
513-675 2.27e-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: 70.40  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   513 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 592
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   593 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 672
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 568950008   673 KGW 675
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
4-380 2.21e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.98  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   4 LVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDASEDQKDEKGYTDHDRK 83
Cdd:COG2203  114 LLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  84 ILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCI 161
Cdd:COG2203  194 LLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLGEGLAGRALRTGEPV 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 162 QLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfptssFTDEDEHVIQHCFHYTGTVLTS 238
Cdd:COG2203  274 VVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-----FTEEDLELLEALADQAAIAIER 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 239 TLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRI 318
Cdd:COG2203  347 ARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLL 423
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950008 319 PADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 380
Cdd:COG2203  424 LDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
93-226 3.10e-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: 50.16  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   93 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 172
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568950008  173 QLQNMLGCELQAMLCVPVISRatDQVVALACAfnklgGDFPTSSFTDEDEHVIQ 226
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLAL-----GSNRPGAFDEEDLELLE 126
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
514-747 1.17e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 311.02  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  514 YHNWMHAFSVSHFCYLLYKNLELSNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 593
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  594 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNRQHHRLLLCLLMTSCDLS 669
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950008  670 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 747
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
268-417 4.06e-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: 4.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   268 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 344
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568950008   345 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 417
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
95-246 3.39e-20

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: 87.82  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008    95 DATSLQLKVLQYLQQETQATHCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 172
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568950008   173 QLQNMLGCEL-QAMLCVPVISRatDQVVALACAFNKLGGDFptssFTDEDEHVIQHCFHYTGTVLTSTLAFQKEQ 246
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRP----FTEEDEELLQALANQLAIALANAQLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
217-428 3.40e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.56  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 217 FTDEDEHVIQHCFHYTGTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQ 296
Cdd:COG2203  156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 297 N--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTG-FRTRNILCFPIKNENqEV 373
Cdd:COG2203  236 DggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDG-RL 311
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568950008 374 IGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANE 428
Cdd:COG2203  312 IGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALAALLQELA 365
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
514-690 8.05e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 83.93  E-value: 8.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 514 YHNWMHAFSVSHFCYLLYKNLELSnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 593
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 594 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNRQHHRLLLCLLMTSCDLSDQTK 673
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 568950008 674 --GWKTTRKIAELIYKEFF 690
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
267-428 1.36e-17

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 81.48  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 267 DDVSVLLQEIITEARNLSNAEICSVFLLDQN----ELVAKVfdgGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 342
Cdd:COG3605   17 LDLDEALDRIVRRIAEALGVDVCSIYLLDPDggrlELRATE---GLNPEAVGKVRLPLGEGLVGLVAERGEPLNLADAAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 343 HPLF-YRGVDDSTGFRTrnILCFPIKNENQeVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 421
Cdd:COG3605   94 HPRFkYFPETGEEGFRS--FLGVPIIRRGR-VLGVLVVQSREPRE-FTEEEVEFLVTLAAQLAEAIANAELLGELRAALA 169

                 ....*..
gi 568950008 422 RSHLANE 428
Cdd:COG3605  170 ELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
268-407 1.87e-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: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  268 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 347
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  348 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 407
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
513-675 2.27e-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: 70.40  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   513 PYHNWMHAFSVSHFCYLLYKNLELSNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 592
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   593 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnrqHHRLLLCLLMTSCDLSDQT 672
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 568950008   673 KGW 675
Cdd:smart00471 116 RAD 118
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
268-408 9.61e-10

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: 57.48  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  268 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVAkvFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFY 347
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568950008  348 RGVDDSTGFRTrnILCFPIKNENqEVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIA 408
Cdd:pfam13185  81 GLPAGHAGLRS--FLSVPLVSGG-RVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
GAF COG2203
GAF domain [Signal transduction mechanisms];
4-380 2.21e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.98  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   4 LVIPLLDKETGSVAAVILVHCGQLSDSEEQSLQVVEKHALVALRRVQALQQRRPEAVQNTSVDASEDQKDEKGYTDHDRK 83
Cdd:COG2203  114 LLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  84 ILQLCGELF--DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCI 161
Cdd:COG2203  194 LLNEISQALrsALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLGEGLAGRALRTGEPV 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 162 QLKDLTSDDV---QQLQNMLGCELQAMLCVPVISRatDQVVALACAFNKLGGDfptssFTDEDEHVIQHCFHYTGTVLTS 238
Cdd:COG2203  274 VVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-----FTEEDLELLEALADQAAIAIER 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 239 TLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRI 318
Cdd:COG2203  347 ARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLL 423
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950008 319 PADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 380
Cdd:COG2203  424 LDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
93-226 3.10e-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: 50.16  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008   93 DLDATSLQLKVLQYLQQETQATHCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPLTMGRLGQVVEDKQCIQLKDLTSDDVQ 172
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568950008  173 QLQNMLGCELQAMLCVPVISRatDQVVALACAfnklgGDFPTSSFTDEDEHVIQ 226
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSG--GRVVGVLAL-----GSNRPGAFDEEDLELLE 126
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
102-226 1.27e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 45.55  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  102 KVLQYLQQETQATHCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLtMGRLGQVVEDKQCIQLKDLTSDD--VQQLQNMLG 179
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIP-PGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568950008  180 CELQAMLCVPVISRatDQVVALACAFNklggdfPTSSFTDEDEHVIQ 226
Cdd:pfam01590  85 FGIRSLLAVPIIDD--GELLGVLVLHH------PRPPFTEEELELLE 123
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
243-394 1.96e-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: 45.59  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008 243 QKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEiitearNLSNAEICSVFLLD-QNELVAKVFDGGVVddesyEIRIPAD 321
Cdd:COG1956    7 EDYDELLAQLSALLAGETDLIANLANISALLFE------ALPDYNWVGFYLVDgGGELVLGPFQGPPA-----CTRIPFG 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568950008 322 QGIAGHVATTGQILNIPDAYAHPLFYRgvDDSTgfrTRNILCFPIKNeNQEVIGVAElvnkINGPWFSKFDED 394
Cdd:COG1956   76 KGVCGTAAAEGETQLVPDVHAFPGHIA--CDSA---SRSEIVVPIFK-DGEVIGVLD----IDSPTPGRFDEE 138
GAF_3 pfam13492
GAF domain;
268-409 2.70e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 44.28  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950008  268 DVSVLLQEIITEARNLSNAEICSVFLLD--QNEL-VAKVFDGGVVDDESyeirIPADQGIAGHVATTGQilnipdayahP 344
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDedGNKLqVAAGYDGEPDPSES----LDADSPLARRALSSGE----------P 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568950008  345 LFYRGVDDSTGFRTRNILCFPIKNENQeVIGVaeLVnkINGPWFSKFDED---LATAFSIYCGISIAH 409
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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