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Conserved domains on  [gi|157364939|ref|NP_006195|]
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cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' [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;
561-805 4.45e-107

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 329.13  E-value: 4.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHG-SSILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDaceqmqtEEEAIKYVTVDPTKKEIIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  720 TACDLSAITKPWEVQSQVALMVANEFWEQGDLERTvLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEIT 799
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 157364939  800 PMLSGL 805
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
80-231 2.71e-26

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: 105.16  E-value: 2.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939    80 VHRALQRLAHLLQADRCSMFLCrSRNGIPEVASRLLDvtptskfedNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVk 159
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLV-DENDRGELVLVAAD---------GLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157364939   160 kNSHFSDFMDKQTGY-VTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSY 231
Cdd:smart00065  75 -EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 2.50e-20

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


:

Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 88.21  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   256 DVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEfydewpiklgevepykgpktpdgrevnfykiidYILHGKEEIKviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---------------------------------LVLVAADGLT--L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   336 TPPADHWTLISGLPTYVAENGFICNMMNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 157364939   416 EHDEYITETLTQFLGWSLLNTDTYDKMN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
561-805 4.45e-107

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 329.13  E-value: 4.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHG-SSILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDaceqmqtEEEAIKYVTVDPTKKEIIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  720 TACDLSAITKPWEVQSQVALMVANEFWEQGDLERTvLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEIT 799
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 157364939  800 PMLSGL 805
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
80-231 2.71e-26

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: 105.16  E-value: 2.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939    80 VHRALQRLAHLLQADRCSMFLCrSRNGIPEVASRLLDvtptskfedNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVk 159
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLV-DENDRGELVLVAAD---------GLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157364939   160 kNSHFSDFMDKQTGY-VTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSY 231
Cdd:smart00065  75 -EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 2.50e-20

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 88.21  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   256 DVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEfydewpiklgevepykgpktpdgrevnfykiidYILHGKEEIKviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---------------------------------LVLVAADGLT--L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   336 TPPADHWTLISGLPTYVAENGFICNMMNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 157364939   416 EHDEYITETLTQFLGWSLLNTDTYDKMN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
76-224 3.71e-14

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: 70.20  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   76 PEQGVHRALQRLAHLLQADRCSMFLCRsrngipevASRLLDVTPTSKFEDNLVGPDKEvvfpldiGIVGWAAHTKKTHNV 155
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPD--------ADGLEYLPPGARWLKAAGLEIPP-------GTGVTVLRTGRPLVV 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157364939  156 PDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKvnASEFSKQDEEVFSKYLNFVSIIL 224
Cdd:pfam01590  67 PDAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
75-269 1.79e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 70.99  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  75 TPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRlldvtptskfednlVGPDKEVV--FPLDIGIVGWAAHTKKT 152
Cdd:COG2203  207 DLEELLQRILELAGELLGADRGAILLVDEDGGELELVAA--------------PGLPEEELgrLPLGEGLAGRALRTGEP 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 153 HNVPDVKKNSHFSDFMDKQTG-YVTKNLLATPIVVGKEVLAVIMAVNKvNASEFSKQDEEVFSKYLNFVSIILRLHHTsy 231
Cdd:COG2203  273 VVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARL-- 349
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157364939 232 mYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVR 269
Cdd:COG2203  350 -YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLE 386
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
560-702 1.38e-09

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: 56.92  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   560 TYHNWRHGFNVGQTMFTLLMTGRLkkyytdLEAFAMLAAAFCHDIDHRGTNNLYQMKstsplarlhgSSILERHHLEYSK 639
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157364939   640 TLLQDESLNIFQNLNKRQFEtvIHLFEVAIIATDLALyfkKRTMFQKIVDACEQMQTEEEAIK 702
Cdd:smart00471  66 ILLEEEEPRILEEILRTAIL--SHHERPDGLRGEPIT---LEARIVKVADRLDALRADRRYRR 123
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
561-746 5.00e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 561 YHNWRHGFNVGQTMFTLLMtgrlKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYqmkstsplarLHGSSILERHHLEYSKT 640
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE----ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 641 LLQDEslnifqnlnkrQFETVIHLFEVAIIATDLALYFKKRTMfqkivdaceqmqteeeaiKYVTVDPTKKEIIMAMMMT 720
Cdd:cd00077   67 ILREL-----------LLEEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 157364939 721 ACDLSAITK--PWEVQSQVALMVANEFW 746
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
336-433 2.08e-04

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: 42.08  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  336 TPPADHWTLISGL------PTYVAENGFICNMMNAPADEYFTFQKGPVDETGwvIKNVLSLPIVNKKEdIVGVATFYNRK 409
Cdd:pfam01590  35 LPPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDDGE-LLGVLVLHHPR 111
                          90       100
                  ....*....|....*....|....
gi 157364939  410 DgkPFDEHDEYITETLTQFLGWSL 433
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
347-454 1.24e-03

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 40.65  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 347 GLPTYVAENGFICNMMNAPADEYFTFqkgpVDETG-WVIKNVLSLPIVNKKEdIVGVATFYNRKDgKPFDEHDEYITETL 425
Cdd:COG3605   74 GLVGLVAERGEPLNLADAASHPRFKY----FPETGeEGFRSFLGVPIIRRGR-VLGVLVVQSREP-REFTEEEVEFLVTL 147
                         90       100
                 ....*....|....*....|....*....
gi 157364939 426 TQFLGWSLLNTDTYDKMNKLENRKDIAQE 454
Cdd:COG3605  148 AAQLAEAIANAELLGELRAALAELSLARE 176
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
561-805 4.45e-107

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 329.13  E-value: 4.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHG-SSILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDaceqmqtEEEAIKYVTVDPTKKEIIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  720 TACDLSAITKPWEVQSQVALMVANEFWEQGDLERTvLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEIT 799
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 157364939  800 PMLSGL 805
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
80-231 2.71e-26

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: 105.16  E-value: 2.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939    80 VHRALQRLAHLLQADRCSMFLCrSRNGIPEVASRLLDvtptskfedNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVk 159
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLV-DENDRGELVLVAAD---------GLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157364939   160 kNSHFSDFMDKQTGY-VTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSY 231
Cdd:smart00065  75 -EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 2.50e-20

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 88.21  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   256 DVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEfydewpiklgevepykgpktpdgrevnfykiidYILHGKEEIKviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---------------------------------LVLVAADGLT--L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   336 TPPADHWTLISGLPTYVAENGFICNMMNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 157364939   416 EHDEYITETLTQFLGWSLLNTDTYDKMN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
76-224 3.71e-14

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: 70.20  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   76 PEQGVHRALQRLAHLLQADRCSMFLCRsrngipevASRLLDVTPTSKFEDNLVGPDKEvvfpldiGIVGWAAHTKKTHNV 155
Cdd:pfam01590   2 LEEILQTILEELRELLGADRCALYLPD--------ADGLEYLPPGARWLKAAGLEIPP-------GTGVTVLRTGRPLVV 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157364939  156 PDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKvnASEFSKQDEEVFSKYLNFVSIIL 224
Cdd:pfam01590  67 PDAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
75-269 1.79e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 70.99  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  75 TPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRlldvtptskfednlVGPDKEVV--FPLDIGIVGWAAHTKKT 152
Cdd:COG2203  207 DLEELLQRILELAGELLGADRGAILLVDEDGGELELVAA--------------PGLPEEELgrLPLGEGLAGRALRTGEP 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 153 HNVPDVKKNSHFSDFMDKQTG-YVTKNLLATPIVVGKEVLAVIMAVNKvNASEFSKQDEEVFSKYLNFVSIILRLHHTsy 231
Cdd:COG2203  273 VVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLELLEALADQAAIAIERARL-- 349
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157364939 232 mYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVR 269
Cdd:COG2203  350 -YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLE 386
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
560-702 1.38e-09

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: 56.92  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939   560 TYHNWRHGFNVGQTMFTLLMTGRLkkyytdLEAFAMLAAAFCHDIDHRGTNNLYQMKstsplarlhgSSILERHHLEYSK 639
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157364939   640 TLLQDESLNIFQNLNKRQFEtvIHLFEVAIIATDLALyfkKRTMFQKIVDACEQMQTEEEAIK 702
Cdd:smart00471  66 ILLEEEEPRILEEILRTAIL--SHHERPDGLRGEPIT---LEARIVKVADRLDALRADRRYRR 123
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
72-214 2.52e-09

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 57.60  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  72 EGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEV-ASRlldvtptskfednlvGPDKEVV----FPLDIGIVGWA 146
Cdd:COG3605   15 SALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELrATE---------------GLNPEAVgkvrLPLGEGLVGLV 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157364939 147 AHTKKTHNVPDVKKNSHFSDF-MDKQTGYVTknLLATPIVVGKEVLAVImAVNKVNASEFSKQDEEVFS 214
Cdd:COG3605   80 AERGEPLNLADAASHPRFKYFpETGEEGFRS--FLGVPIIRRGRVLGVL-VVQSREPREFTEEEVEFLV 145
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
561-746 5.00e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 561 YHNWRHGFNVGQTMFTLLMtgrlKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYqmkstsplarLHGSSILERHHLEYSKT 640
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE----ELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 641 LLQDEslnifqnlnkrQFETVIHLFEVAIIATDLALYFKKRTMfqkivdaceqmqteeeaiKYVTVDPTKKEIIMAMMMT 720
Cdd:cd00077   67 ILREL-----------LLEEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 157364939 721 ACDLSAITK--PWEVQSQVALMVANEFW 746
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
336-433 2.08e-04

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: 42.08  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  336 TPPADHWTLISGL------PTYVAENGFICNMMNAPADEYFTFQKGPVDETGwvIKNVLSLPIVNKKEdIVGVATFYNRK 409
Cdd:pfam01590  35 LPPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDDGE-LLGVLVLHHPR 111
                          90       100
                  ....*....|....*....|....
gi 157364939  410 DgkPFDEHDEYITETLTQFLGWSL 433
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
134-226 3.66e-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: 41.74  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 134 VVFPLDIGIVGWAAHTKKTHNVPDVkknshfsdfmDKQTGYV-----TKNLLATPIVVGKEVLAVI-MAVNKVNAseFSK 207
Cdd:COG1956   70 TRIPFGKGVCGTAAAEGETQLVPDV----------HAFPGHIacdsaSRSEIVVPIFKDGEVIGVLdIDSPTPGR--FDE 137
                         90
                 ....*....|....*....
gi 157364939 208 QDEEVFSKylnFVSIILRL 226
Cdd:COG1956  138 EDQAGLEA---LAALLAEA 153
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
133-225 1.15e-03

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: 40.14  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939  133 EVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYvtKNLLATPIVVGKEVLAVImAVNKVNASEFSKQDEEV 212
Cdd:pfam13185  48 ALDDPPGEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVGVL-ALGSNRPGAFDEEDLEL 124
                          90
                  ....*....|...
gi 157364939  213 FSKYLNFVSIILR 225
Cdd:pfam13185 125 LELLAEQAAIAIE 137
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
347-454 1.24e-03

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 40.65  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157364939 347 GLPTYVAENGFICNMMNAPADEYFTFqkgpVDETG-WVIKNVLSLPIVNKKEdIVGVATFYNRKDgKPFDEHDEYITETL 425
Cdd:COG3605   74 GLVGLVAERGEPLNLADAASHPRFKY----FPETGeEGFRSFLGVPIIRRGR-VLGVLVVQSREP-REFTEEEVEFLVTL 147
                         90       100
                 ....*....|....*....|....*....
gi 157364939 426 TQFLGWSLLNTDTYDKMNKLENRKDIAQE 454
Cdd:COG3605  148 AAQLAEAIANAELLGELRAALAELSLARE 176
 
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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