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Conserved domains on  [gi|319748276|gb|ADV69111|]
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dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A transcript variant 4 [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;
663-898 2.88e-116

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.93  E-value: 2.88e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  663 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319748276  820 VTKPWEISRQVAELVTSEFFKQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 5.59e-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: 5.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsstensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 319748276   377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 1.42e-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: 92.06  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   482 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 319748276   562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
663-898 2.88e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.93  E-value: 2.88e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  663 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319748276  820 VTKPWEISRQVAELVTSEFFKQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 5.59e-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: 5.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsstensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 319748276   377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 1.42e-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: 92.06  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   482 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 319748276   562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
203-549 4.00e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.95  E-value: 4.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 203 QFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEgaaAGKKTLVSKffdVHAGTPLlpcsstenSNEVQVPW 282
Cdd:COG2203  193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD---EDGGELELV---AAPGLPE--------EELGRLPL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 283 GKGIIGYVGEHGETVNIPDAYQDRRFND-EIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKipEGAPFTEDDEKVMQM 361
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRFAPsLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSK--EPRAFTEEDLELLEA 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 362 YLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKS 441
Cdd:COG2203  336 LADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGL 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 442 FELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSN 521
Cdd:COG2203  416 LALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLL 495
                        330       340
                 ....*....|....*....|....*...
gi 319748276 522 HQIIGVAQVLNRLDGKPFDDADQRLFEA 549
Cdd:COG2203  496 ALLALSALAVLASLLLALLLLLLLLLLL 523
GAF COG2203
GAF domain [Signal transduction mechanisms];
368-574 1.72e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 90.64  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 368 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 447
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 448 KCSADAENSFKESMEkssysdwlINNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 526
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 319748276 527 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 574
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
200-391 2.73e-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: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 200 NERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAaagKKTLVskffdvhagtpllpCSSTENSNE-- 277
Cdd:COG3605    1 EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPD---GGRLE--------------LRATEGLNPea 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 278 ---VQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNdEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKipEGAPFTED 354
Cdd:COG3605   64 vgkVRLPLGEGLVGLVAERGEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSR--EPREFTEE 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 319748276 355 DEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 391
Cdd:COG3605  140 EVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
217-370 1.72e-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: 76.75  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  217 DLTSLSYKILIFVCLMVDADRCSLFLvegaaagkktlvskfFDVHAGTPLLPCSSTENSNEVQVPWGKGIigYVGEHGET 296
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYL---------------PDADGLEYLPPGARWLKAAGLEIPPGTGV--TVLRTGRP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319748276  297 VNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKIPegaPFTEDDEKVMQMYLPFCGIAI 370
Cdd:pfam01590  64 LVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
402-558 1.92e-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: 76.75  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESMEKSsysdwlinNSIAELVAS 481
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319748276  482 TGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 558
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
663-839 1.37e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 60.43  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 663 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 742
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 743 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGEYDWNIKNHRDIFRSMLMTACDL--GAV 820
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 319748276 821 TKPWEISRQVAELVTSEFF 839
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
663-759 3.29e-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: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   663 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 742
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 319748276   743 MILQSEGHNIFANLSSK 759
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
663-898 2.88e-116

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 354.93  E-value: 2.88e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  663 YHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSALAQLYGTSATLEHHHFNHAV 742
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  743 MILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVSKGE---YDWNIKNHRDIFRSMLMTACDLGA 819
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319748276  820 VTKPWEISRQVAELVTSEFFKQGDRERlELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSV 898
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEK-ELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
217-380 5.59e-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: 5.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   217 DLTSLSYKILIFVCLMVDADRCSLFLVEgaAAGKKTLVSKFFDVHAGTPLlpcsstensnEVQVPWGKGIIGYVGEHGET 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVD--ENDRGELVLVAADGLTLPTL----------GIRFPLDEGLAGRVAETGRP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   297 VNIPDAYQDRRFNDEIDKLTGyKTKSLLCMPIRSsDGEIIGVAQAINKiPEGAPFTEDDEKVMQMYLPFCGIAISNAQLF 376
Cdd:smart00065  69 LNIPDVEADPLFAEDLLGRYQ-GVRSFLAVPLVA-DGELVGVLALHNK-KSPRPFTEEDEELLQALANQLAIALANAQLY 145

                   ....
gi 319748276   377 AASR 380
Cdd:smart00065 146 EELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
402-568 1.42e-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: 92.06  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkFTKSFELMSPKCSADAensfkesmekssysdWLINNSIAELVAS 481
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGEL-VLVAADGLTLPTLGIR---------------FPLDEGLAGRVAE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   482 TGLPVNISDAYQDPRFDAEADQISGFhIRSVLCVPIWNsNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNT 561
Cdd:smart00065  65 TGRPLNIPDVEADPLFAEDLLGRYQG-VRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 319748276   562 IMYDQVK 568
Cdd:smart00065 143 QLYEELR 149
GAF COG2203
GAF domain [Signal transduction mechanisms];
203-549 4.00e-19

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 92.95  E-value: 4.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 203 QFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEgaaAGKKTLVSKffdVHAGTPLlpcsstenSNEVQVPW 282
Cdd:COG2203  193 ALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD---EDGGELELV---AAPGLPE--------EELGRLPL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 283 GKGIIGYVGEHGETVNIPDAYQDRRFND-EIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKipEGAPFTEDDEKVMQM 361
Cdd:COG2203  259 GEGLAGRALRTGEPVVVNDASTDPRFAPsLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSK--EPRAFTEEDLELLEA 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 362 YLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKS 441
Cdd:COG2203  336 LADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGL 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 442 FELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVASTGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSN 521
Cdd:COG2203  416 LALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLL 495
                        330       340
                 ....*....|....*....|....*...
gi 319748276 522 HQIIGVAQVLNRLDGKPFDDADQRLFEA 549
Cdd:COG2203  496 ALLALSALAVLASLLLALLLLLLLLLLL 523
GAF COG2203
GAF domain [Signal transduction mechanisms];
368-574 1.72e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 90.64  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 368 IAISNAQLFAASRKEYERSRALLEVVNDLFEEqTDLEKIVKKIMHRAQTLLKCERCSVLLLEDiespvvkftkSFELMSP 447
Cdd:COG2203  174 ILDIARLLTQRARLELERLALLNEISQALRSA-LDLEELLQRILELAGELLGADRGAILLVDE----------DGGELEL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 448 KCSADAENSFKESMEkssysdwlINNSIAELVASTGLPVNISDAYQDPRF-DAEADQISGFHIRSVLCVPIWNSNhQIIG 526
Cdd:COG2203  243 VAAPGLPEEELGRLP--------LGEGLAGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLVDG-RLIG 313
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 319748276 527 VAQVLNRLDGkPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQ 574
Cdd:COG2203  314 VLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAAL 360
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
200-391 2.73e-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: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 200 NERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAaagKKTLVskffdvhagtpllpCSSTENSNE-- 277
Cdd:COG3605    1 EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPD---GGRLE--------------LRATEGLNPea 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 278 ---VQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNdEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKipEGAPFTED 354
Cdd:COG3605   64 vgkVRLPLGEGLVGLVAERGEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSR--EPREFTEE 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 319748276 355 DEKVMQ---MYLpfcGIAISNAQLFAASRKEYERSRALLE 391
Cdd:COG3605  140 EVEFLVtlaAQL---AEAIANAELLGELRAALAELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
217-370 1.72e-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: 76.75  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  217 DLTSLSYKILIFVCLMVDADRCSLFLvegaaagkktlvskfFDVHAGTPLLPCSSTENSNEVQVPWGKGIigYVGEHGET 296
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYL---------------PDADGLEYLPPGARWLKAAGLEIPPGTGV--TVLRTGRP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319748276  297 VNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRsSDGEIIGVAQAINKIPegaPFTEDDEKVMQMYLPFCGIAI 370
Cdd:pfam01590  64 LVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP---PFTEEELELLEVLADQVAIAL 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
402-558 1.92e-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: 76.75  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmspkcSADAENSFKESMEKSsysdwlinNSIAELVAS 481
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL-------------PPGARWLKAAGLEIP--------PGTGVTVLR 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319748276  482 TGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNsNHQIIGVAQVLNRldGKPFDDADQRLFEAFVIFCGLGI 558
Cdd:pfam01590  60 TGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
387-568 8.04e-14

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 70.70  E-value: 8.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 387 RALLEVVNDLfEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLeDIEspvvkfTKSFELMSpkcsadAENSFKESMEKSSY 466
Cdd:COG3605    4 KALRRISEAV-ASALDLDEALDRIVRRIAEALGVDVCSIYLL-DPD------GGRLELRA------TEGLNPEAVGKVRL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 467 SdwlINNSIAELVASTGLPVNISDAYQDPRFdAEADQISGFHIRSVLCVPIwNSNHQIIGVAQVLNRlDGKPFDDADQRL 546
Cdd:COG3605   70 P---LGEGLVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPI-IRRGRVLGVLVVQSR-EPREFTEEEVEF 143
                        170       180
                 ....*....|....*....|..
gi 319748276 547 FEAFVIFCGLGINNTIMYDQVK 568
Cdd:COG3605  144 LVTLAAQLAEAIANAELLGELR 165
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
663-839 1.37e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 60.43  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 663 YHNWRHAFNVCQLMFAMLTTAGfqdiLTEVEILAVIVGCLCHDLDHRGTNNAFqaksgsalaqlYGTSATLEHHHFNHAV 742
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 743 MILQSEghnifanlsskEYSDLMQLLKQSILATDLtlyferrtEFFELVSKGEYDWNIKNHRDIFRSMLMTACDL--GAV 820
Cdd:cd00077   66 EILREL-----------LLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRldALR 126
                        170
                 ....*....|....*....
gi 319748276 821 TKPWEISRQVAELVTSEFF 839
Cdd:cd00077  127 RDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
663-759 3.29e-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: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276   663 YHNWRHAFNVCQLMFAMLttagfqDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSGSalaqlygtsatLEHHHFNHAV 742
Cdd:smart00471   3 YHVFEHSLRVAQLAAALA------EELGLLDIELLLLAALLHDIGKPGTPDSFLVKTSV-----------LEDHHFIGAE 65
                           90
                   ....*....|....*..
gi 319748276   743 MILQSEGHNIFANLSSK 759
Cdd:smart00471  66 ILLEEEEPRILEEILRT 82
GAF_3 pfam13492
GAF domain;
402-550 4.22e-10

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 58.54  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276  402 DLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVkftksfelmsPKCSADAENSFKESMEkssysdwlINNSIAELVAS 481
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDEDGNKLQ----------VAAGYDGEPDPSESLD--------ADSPLARRALS 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319748276  482 TGLPVnisdayqdprFDAEADQISGFHIRSVLCVPIwNSNHQIIGVAqVLNRLDGKPFDDADQRLFEAF 550
Cdd:pfam13492  63 SGEPI----------SGLGSAGEDGLPDGPALVVPL-VAGRRVIGVL-ALASSKPRAFDAEDLRLLESL 119
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
278-360 4.38e-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: 53.29  E-value: 4.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 278 VQVPWGKGIIGYVGEHGETVNIPDAYQDrrfndeidklTGY-----KTKSLLCMPIRsSDGEIIGVaqaINkI--PEGAP 350
Cdd:COG1956   70 TRIPFGKGVCGTAAAEGETQLVPDVHAF----------PGHiacdsASRSEIVVPIF-KDGEVIGV---LD-IdsPTPGR 134
                         90
                 ....*....|
gi 319748276 351 FTEDDEKVMQ 360
Cdd:COG1956  135 FDEEDQAGLE 144
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
479-551 6.46e-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: 41.35  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319748276 479 VASTGLPVNISDAYQDPRfdaeadqisgfHI------RSVLCVPIWNsNHQIIGV----AQVLNRldgkpFDDADQRLFE 548
Cdd:COG1956   82 AAAEGETQLVPDVHAFPG-----------HIacdsasRSEIVVPIFK-DGEVIGVldidSPTPGR-----FDEEDQAGLE 144

                 ...
gi 319748276 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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