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Conserved domains on  [gi|18266694|ref|NP_543169|]
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dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A isoform 4 [Rattus norvegicus]

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;
663-898 4.18e-116

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.55  E-value: 4.18e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   663 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18266694   820 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 6.00e-25

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: 101.69  E-value: 6.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsttensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 18266694    377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 4.54e-21

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: 90.52  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    482 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 18266694    562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
663-898 4.18e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.55  E-value: 4.18e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   663 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18266694   820 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 6.00e-25

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: 101.69  E-value: 6.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsttensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 18266694    377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 4.54e-21

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: 90.52  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    482 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 18266694    562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
200-391 2.98e-18

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 83.79  E-value: 2.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 200 NERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAaagKKTLVskffdvhagtpllpCSTTENSNE-- 277
Cdd:COG3605   1 EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPD---GGRLE--------------LRATEGLNPea 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 278 ---VQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNdEIDKLTGYKTKSLLCMPIRnSDGEIIGVAQAINKVPEgaPFTED 354
Cdd:COG3605  64 vgkVRLPLGEGLVGLVAERGEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSREPR--EFTEE 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18266694 355 DEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 391
Cdd:COG3605 140 EVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
GAF COG2203
GAF domain [Signal transduction mechanisms];
203-549 5.91e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.10  E-value: 5.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 203 QFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEgaaAGKKTLVSKffdVHAGTPLlpcsttenSNEVQVPW 282
Cdd:COG2203 193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD---EDGGELELV---AAPGLPE--------EELGRLPL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 283 GKGIIGYVGEHGETVNIPDAYQDRRFND-EIDKLTGYKTKSLLCMPIRnSDGEIIGVAQAINKVPegAPFTEDDEKVMQM 361
Cdd:COG2203 259 GEGLAGRALRTGEPVVVNDASTDPRFAPsLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEP--RAFTEEDLELLEA 335
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 362 YLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKS 441
Cdd:COG2203 336 LADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGL 415
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 442 FELMSPKCSADAENSFKESVEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSN 521
Cdd:COG2203 416 LALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLL 495
                       330       340
                ....*....|....*....|....*...
gi 18266694 522 HQIIGVAQVLNRLDGKPFDDADQRLFEA 549
Cdd:COG2203 496 ALLALSALAVLASLLLALLLLLLLLLLL 523
GAF COG2203
GAF domain [Signal transduction mechanisms];
368-574 5.27e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 86.02  E-value: 5.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 368 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 447
Cdd:COG2203 174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 448 KCSADAENSFKESVEkssysdwlINNSIAELVASTGLPVNVSDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 526
Cdd:COG2203 243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18266694 527 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 574
Cdd:COG2203 314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
402-558 2.62e-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: 76.36  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESVEKSsysdwlinNSIAELVAS 481
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18266694   482 TGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 558
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
217-370 2.78e-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: 76.36  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   217 DLTSLSYKILIFVCLMVDADRCSLFLvegaaagkktlvskfFDVHAGTPLLPCSTTENSNEVQVPWGKGIigYVGEHGET 296
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYL---------------PDADGLEYLPPGARWLKAAGLEIPPGTGV--TVLRTGRP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18266694   297 VNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRNsDGEIIGVAQAINKVPegaPFTEDDEKVMQMYLPFCGIAI 370
Cdd:pfam01590  64 LVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
663-759 3.96e-10

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: 58.46  E-value: 3.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    663 YHNWRHAFNVCQLMFAMLttagfqEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSalaqlygtsatLEHHHFNHAV 742
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 18266694    743 MILQSEGHNIFANLSSK 759
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
663-839 6.42e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.50  E-value: 6.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 663 YHNWRHAFNVCQLMFAMlttaGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFqaksdsalaqlYGTSATLEHHHFNHAV 742
Cdd:cd00077   1 EHRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 743 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGAYDWSITSHRDVFRSMLMTACDL--GAV 820
Cdd:cd00077  66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                       170
                ....*....|....*....
gi 18266694 821 TKPWEISRQVAELVTSEFF 839
Cdd:cd00077 127 RDSREKRRRIAEEDLEELL 145
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
663-898 4.18e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.55  E-value: 4.18e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   663 YHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGA---YDWSITSHRDVFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18266694   820 VTKPWEISRQVAELVTSEFFEQGDRERsELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 6.00e-25

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: 101.69  E-value: 6.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsttensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRNsDGEIIGVAQAINKVpEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNKK-SPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 18266694    377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 4.54e-21

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: 90.52  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesvekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    482 TGLPVNVSDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 18266694    562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
200-391 2.98e-18

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 83.79  E-value: 2.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 200 NERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAaagKKTLVskffdvhagtpllpCSTTENSNE-- 277
Cdd:COG3605   1 EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPD---GGRLE--------------LRATEGLNPea 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 278 ---VQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNdEIDKLTGYKTKSLLCMPIRnSDGEIIGVAQAINKVPEgaPFTED 354
Cdd:COG3605  64 vgkVRLPLGEGLVGLVAERGEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSREPR--EFTEE 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18266694 355 DEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 391
Cdd:COG3605 140 EVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
GAF COG2203
GAF domain [Signal transduction mechanisms];
203-549 5.91e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.10  E-value: 5.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 203 QFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEgaaAGKKTLVSKffdVHAGTPLlpcsttenSNEVQVPW 282
Cdd:COG2203 193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD---EDGGELELV---AAPGLPE--------EELGRLPL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 283 GKGIIGYVGEHGETVNIPDAYQDRRFND-EIDKLTGYKTKSLLCMPIRnSDGEIIGVAQAINKVPegAPFTEDDEKVMQM 361
Cdd:COG2203 259 GEGLAGRALRTGEPVVVNDASTDPRFAPsLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEP--RAFTEEDLELLEA 335
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 362 YLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKS 441
Cdd:COG2203 336 LADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGL 415
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 442 FELMSPKCSADAENSFKESVEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSN 521
Cdd:COG2203 416 LALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLL 495
                       330       340
                ....*....|....*....|....*...
gi 18266694 522 HQIIGVAQVLNRLDGKPFDDADQRLFEA 549
Cdd:COG2203 496 ALLALSALAVLASLLLALLLLLLLLLLL 523
GAF COG2203
GAF domain [Signal transduction mechanisms];
368-574 5.27e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 86.02  E-value: 5.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 368 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 447
Cdd:COG2203 174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 448 KCSADAENSFKESVEkssysdwlINNSIAELVASTGLPVNVSDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 526
Cdd:COG2203 243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18266694 527 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 574
Cdd:COG2203 314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
402-558 2.62e-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: 76.36  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESVEKSsysdwlinNSIAELVAS 481
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18266694   482 TGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 558
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
217-370 2.78e-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: 76.36  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   217 DLTSLSYKILIFVCLMVDADRCSLFLvegaaagkktlvskfFDVHAGTPLLPCSTTENSNEVQVPWGKGIigYVGEHGET 296
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYL---------------PDADGLEYLPPGARWLKAAGLEIPPGTGV--TVLRTGRP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18266694   297 VNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRNsDGEIIGVAQAINKVPegaPFTEDDEKVMQMYLPFCGIAI 370
Cdd:pfam01590  64 LVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
387-579 3.38e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 71.85  E-value: 3.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 387 RALLEVVNDLfEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLeDIEspvvkfTKSFELMSpkcsadAENSFKESVEKSSY 466
Cdd:COG3605   4 KALRRISEAV-ASALDLDEALDRIVRRIAEALGVDVCSIYLL-DPD------GGRLELRA------TEGLNPEAVGKVRL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 467 SdwlINNSIAELVASTGLPVNVSDAYQDPRFdAEADQISGFHIRSVLCVPIwNSNHQIIGVAQVLNRlDGKPFDDADQRL 546
Cdd:COG3605  70 P---LGEGLVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPI-IRRGRVLGVLVVQSR-EPREFTEEEVEF 143
                       170       180       190
                ....*....|....*....|....*....|...
gi 18266694 547 FEAFVIFCGLGINNTIMYDQVKKSWAKQSVALD 579
Cdd:COG3605 144 LVTLAAQLAEAIANAELLGELRAALAELSLARE 176
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
663-759 3.96e-10

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: 58.46  E-value: 3.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694    663 YHNWRHAFNVCQLMFAMLttagfqEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSalaqlygtsatLEHHHFNHAV 742
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 18266694    743 MILQSEGHNIFANLSSK 759
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
663-839 6.42e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.50  E-value: 6.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 663 YHNWRHAFNVCQLMFAMlttaGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFqaksdsalaqlYGTSATLEHHHFNHAV 742
Cdd:cd00077   1 EHRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 743 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGAYDWSITSHRDVFRSMLMTACDL--GAV 820
Cdd:cd00077  66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                       170
                ....*....|....*....
gi 18266694 821 TKPWEISRQVAELVTSEFF 839
Cdd:cd00077 127 RDSREKRRRIAEEDLEELL 145
GAF_3 pfam13492
GAF domain;
402-550 1.02e-09

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 57.38  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmsPKCSADAENSFKESVEkssysdwlINNSIAELVAS 481
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDEDGNKLQ----------VAAGYDGEPDPSESLD--------ADSPLARRALS 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18266694   482 TGLPVNVsdayqdprfdAEADQISGFHIRSVLCVPIwNSNHQIIGVAqVLNRLDGKPFDDADQRLFEAF 550
Cdd:pfam13492  63 SGEPISG----------LGSAGEDGLPDGPALVVPL-VAGRRVIGVL-ALASSKPRAFDAEDLRLLESL 119
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
278-360 3.23e-08

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


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 53.68  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 278 VQVPWGKGIIGYVGEHGETVNIPDAYQDrrfndeidklTGY-----KTKSLLCMPIRNsDGEIIGVaqaINkV--PEGAP 350
Cdd:COG1956  70 TRIPFGKGVCGTAAAEGETQLVPDVHAF----------PGHiacdsASRSEIVVPIFK-DGEVIGV---LD-IdsPTPGR 134
                        90
                ....*....|
gi 18266694 351 FTEDDEKVMQ 360
Cdd:COG1956 135 FDEEDQAGLE 144
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
479-551 2.89e-04

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


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 42.12  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266694 479 VASTGLPVNVSDAYQDPRfdaeadqisgfHI------RSVLCVPIWNsNHQIIGV----AQVLNRldgkpFDDADQRLFE 548
Cdd:COG1956  82 AAAEGETQLVPDVHAFPG-----------HIacdsasRSEIVVPIFK-DGEVIGVldidSPTPGR-----FDEEDQAGLE 144

                ...
gi 18266694 549 AFV 551
Cdd:COG1956 145 ALA 147
 
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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