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Conserved domains on  [gi|4505657|ref|NP_002590|]
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cGMP-dependent 3',5'-cyclic phosphodiesterase isoform PDE2A3 [Homo sapiens]

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;
655-888 6.54e-102

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 317.57  E-value: 6.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    655 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 734
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    735 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 810
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505657    811 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 888
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
409-558 5.34e-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: 5.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     409 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 485
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505657     486 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 558
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
241-387 9.24e-18

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: 80.89  E-value: 9.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     241 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 317
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505657     318 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 387
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
655-888 6.54e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 317.57  E-value: 6.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    655 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 734
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    735 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 810
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505657    811 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 888
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
409-558 5.34e-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: 5.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     409 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 485
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505657     486 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 558
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
655-831 2.09e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.47  E-value: 2.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  655 YHNWMHAFSVSHFCYLLYKNLELTnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 734
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  735 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTK 814
Cdd:cd00077  65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                       170
                ....*....|....*....
gi 4505657  815 --GWKTTRKIAELIYKEFF 831
Cdd:cd00077 127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
326-569 1.70e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 90.64  E-value: 1.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  326 ELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFT 405
Cdd:COG2203 124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALR 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  406 HLDDVSVLLQEIITEARNLSNAEICSVFLLDQN--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 483
Cdd:COG2203 204 SALDLEELLQRILELAGELLGADRGAILLVDEDggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDAST 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  484 HPLFYRGVDDSTG-FRTRNILCFPIKNENqEVIGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 562
Cdd:COG2203 281 DPRFAPSLRELLLaLGIRSLLCVPLLVDG-RLIGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALA 358

                ....*..
gi 4505657  563 RSHLANE 569
Cdd:COG2203 359 ALLQELA 365
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
241-387 9.24e-18

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: 80.89  E-value: 9.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     241 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 317
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505657     318 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 387
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
409-548 3.20e-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: 75.98  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    409 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 488
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    489 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 548
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
654-816 1.10e-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: 71.56  E-value: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     654 PYHNWMHAFSVSHFCYLLYKNLELTNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 733
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     734 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnkqHHRLLLCLLMTSCDLSDQT 813
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 4505657     814 KGW 816
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
131-521 4.55e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.21  E-value: 4.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  131 PLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPP 210
Cdd:COG2203  95 LVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLI 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  211 EGTAEDQKGGAAYTDRDRKILQLCGE--LYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEV 288
Cdd:COG2203 175 LDIARLLTQRARLELERLALLNEISQalRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELG 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  289 SFPL-TGCLGQVVEDKKSIQLKDLTSEDV---QQLQSMLGCELQAMLCVPVISRatDQVVALACAFNKLEGDlFTDEDEH 364
Cdd:COG2203 255 RLPLgEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLE 331
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  365 VIQHCFHYTSTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKV 444
Cdd:COG2203 332 LLEALADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLD 408
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505657  445 FDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 521
Cdd:COG2203 409 AADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
248-367 7.09e-07

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: 49.40  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    248 KVLQYLQQETRASRCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSED--VQQLQSMLGC 325
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRNF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 4505657    326 ELQAMLCVPVISRatDQVVALACAFNKleGDLFTDEDEHVIQ 367
Cdd:pfam01590  86 GIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
655-888 6.54e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 317.57  E-value: 6.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    655 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 734
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    735 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 810
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505657    811 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 888
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
409-558 5.34e-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: 5.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     409 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 485
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505657     486 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 558
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
655-831 2.09e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.47  E-value: 2.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  655 YHNWMHAFSVSHFCYLLYKNLELTnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 734
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  735 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTK 814
Cdd:cd00077  65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                       170
                ....*....|....*....
gi 4505657  815 --GWKTTRKIAELIYKEFF 831
Cdd:cd00077 127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
326-569 1.70e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 90.64  E-value: 1.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  326 ELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFT 405
Cdd:COG2203 124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALR 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  406 HLDDVSVLLQEIITEARNLSNAEICSVFLLDQN--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 483
Cdd:COG2203 204 SALDLEELLQRILELAGELLGADRGAILLVDEDggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDAST 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  484 HPLFYRGVDDSTG-FRTRNILCFPIKNENqEVIGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 562
Cdd:COG2203 281 DPRFAPSLRELLLaLGIRSLLCVPLLVDG-RLIGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALA 358

                ....*..
gi 4505657  563 RSHLANE 569
Cdd:COG2203 359 ALLQELA 365
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
241-387 9.24e-18

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: 80.89  E-value: 9.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     241 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 317
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505657     318 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 387
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
408-569 4.25e-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: 4.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  408 DDVSVLLQEIITEARNLSNAEICSVFLLDQN----ELVAKVfdgGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 483
Cdd:COG3605  17 LDLDEALDRIVRRIAEALGVDVCSIYLLDPDggrlELRATE---GLNPEAVGKVRLPLGEGLVGLVAERGEPLNLADAAS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  484 HPLF-YRGVDDSTGFRTrnILCFPIKNENQeVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 562
Cdd:COG3605  94 HPRFkYFPETGEEGFRS--FLGVPIIRRGR-VLGVLVVQSREPRE-FTEEEVEFLVTLAAQLAEAIANAELLGELRAALA 169

                ....*..
gi 4505657  563 RSHLANE 569
Cdd:COG3605 170 ELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
409-548 3.20e-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: 75.98  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    409 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 488
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    489 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 548
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
654-816 1.10e-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: 71.56  E-value: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     654 PYHNWMHAFSVSHFCYLLYKNLELTNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 733
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657     734 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnkqHHRLLLCLLMTSCDLSDQT 813
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 4505657     814 KGW 816
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 ...
409-549 2.11e-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: 56.71  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    409 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVAkvFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFY 488
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505657    489 RGVDDSTGFRTrnILCFPIKNENqEVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIA 549
Cdd:pfam13185  81 GLPAGHAGLRS--FLSVPLVSGG-RVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
GAF COG2203
GAF domain [Signal transduction mechanisms];
131-521 4.55e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.21  E-value: 4.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  131 PLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPP 210
Cdd:COG2203  95 LVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLI 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  211 EGTAEDQKGGAAYTDRDRKILQLCGE--LYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEV 288
Cdd:COG2203 175 LDIARLLTQRARLELERLALLNEISQalRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELG 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  289 SFPL-TGCLGQVVEDKKSIQLKDLTSEDV---QQLQSMLGCELQAMLCVPVISRatDQVVALACAFNKLEGDlFTDEDEH 364
Cdd:COG2203 255 RLPLgEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FTEEDLE 331
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  365 VIQHCFHYTSTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKV 444
Cdd:COG2203 332 LLEALADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLD 408
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505657  445 FDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELV 521
Cdd:COG2203 409 AADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
248-367 7.09e-07

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: 49.40  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    248 KVLQYLQQETRASRCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSED--VQQLQSMLGC 325
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRNF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 4505657    326 ELQAMLCVPVISRatDQVVALACAFNKleGDLFTDEDEHVIQ 367
Cdd:pfam01590  86 GIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
389-535 2.73e-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: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657  389 LKCECQALLQVAKNLFTHLDDVSVLLQEiitearNLSNAEICSVFLLD-QNELVAKVFDGGVVddesyEIRIPADQGIAG 467
Cdd:COG1956  12 LLAQLSALLAGETDLIANLANISALLFE------ALPDYNWVGFYLVDgGGELVLGPFQGPPA-----CTRIPFGKGVCG 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505657  468 HVATTGQILNIPDAYAHPLFYRgvDDSTgfrTRNILCFPIKNeNQEVIGVAElvnkINGPWFSKFDED 535
Cdd:COG1956  81 TAAAEGETQLVPDVHAFPGHIA--CDSA---SRSEIVVPIFK-DGEVIGVLD----IDSPTPGRFDEE 138
GAF_3 pfam13492
GAF domain;
409-550 6.84e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 43.51  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    409 DVSVLLQEIITEARNLSNAEICSVFLLD--QNEL-VAKVFDGGVVDDESyeirIPADQGIAGHVATTGQilnipdayahP 485
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDedGNKLqVAAGYDGEPDPSES----LDADSPLARRALSSGE----------P 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505657    486 LFYRGVDDSTGFRTRNILCFPIKNENQeVIGVaeLVnkINGPWFSKFDED---LATAFSIYCGISIAH 550
Cdd:pfam13492  67 ISGLGSAGEDGLPDGPALVVPLVAGRR-VIGV--LA--LASSKPRAFDAEdlrLLESLAAQIATAIEN 129
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
249-367 9.49e-05

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: 43.22  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505657    249 VLQYLQQETRASRCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPL-TGCLGQVVEDKKSIQLKDLTSEDVQQLQSMLGCEL 327
Cdd:pfam13185  11 VLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPgEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGL 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 4505657    328 QAMLCVPVISRatDQVVALACAFNKLEGDlFTDEDEHVIQ 367
Cdd:pfam13185  90 RSFLSVPLVSG--GRVVGVLALGSNRPGA-FDEEDLELLE 126
 
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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