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Conserved domains on  [gi|284005078|ref|NP_001164430|]
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cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' isoform 2 [Mus musculus]

Protein Classification

3',5'-cyclic nucleotide phosphodiesterase( domain architecture ID 10637639)

3',5'-cyclic nucleotide phosphodiesterase catalyzes the hydrolysis of cAMP or cGMP to produce adenosine 5'-phosphate or guanosine 5'-phosphate, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
561-780 1.97e-91

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.52  E-value: 1.97e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGT-SILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDtceqmqsEEETIKYVTSDPTKKEVIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  720 TACDLSAITKPWEVQSQ------------------------PMMDRSKKDELPKLQVGFIDFVCTFVYKEFSRFHGEITP 775
Cdd:pfam00233 154 KAADISNPTRPWEISKKwadlvaeeffrqgdlekelglpvsPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQP 233

                  ....*
gi 284005078  776 MLNGL 780
Cdd:pfam00233 234 LLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
81-232 3.44e-22

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: 93.60  E-value: 3.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078    81 HRALQRLAQLLQADCCSMFSCRaRNGIPEVASRLLnvtptskfeDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVkk 160
Cdd:smart00065   7 QTILEELRQLLGADRVLIYLVD-ENDRGELVLVAA---------DGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV-- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284005078   161 NSHFSDFMDKQTGY-VTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYL 232
Cdd:smart00065  75 EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 3.47e-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: 3.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   256 DVERQFHKALYTIRTYLNCDRYSIGLLDMtkekefydewpiklgevepykgpktpDGREIIFYKIIDYILhgkeeinviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDE--------------------------NDRGELVLVAADGLT---------L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   336 SPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 284005078   416 EHDEHITETLTQFLGWSLLNTDTYERVN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
561-780 1.97e-91

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.52  E-value: 1.97e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGT-SILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDtceqmqsEEETIKYVTSDPTKKEVIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  720 TACDLSAITKPWEVQSQ------------------------PMMDRSKKDELPKLQVGFIDFVCTFVYKEFSRFHGEITP 775
Cdd:pfam00233 154 KAADISNPTRPWEISKKwadlvaeeffrqgdlekelglpvsPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQP 233

                  ....*
gi 284005078  776 MLNGL 780
Cdd:pfam00233 234 LLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
81-232 3.44e-22

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: 93.60  E-value: 3.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078    81 HRALQRLAQLLQADCCSMFSCRaRNGIPEVASRLLnvtptskfeDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVkk 160
Cdd:smart00065   7 QTILEELRQLLGADRVLIYLVD-ENDRGELVLVAA---------DGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV-- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284005078   161 NSHFSDFMDKQTGY-VTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYL 232
Cdd:smart00065  75 EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 3.47e-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: 3.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   256 DVERQFHKALYTIRTYLNCDRYSIGLLDMtkekefydewpiklgevepykgpktpDGREIIFYKIIDYILhgkeeinviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDE--------------------------NDRGELVLVAADGLT---------L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   336 SPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 284005078   416 EHDEHITETLTQFLGWSLLNTDTYERVN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
77-224 2.86e-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: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   77 EQMAHRALQRLAQLLQADCCSMFSCRArngipevaSRLLNVTPTSKFEDNLVAPDREvvfpldiGIVGWVAHVKKALNVS 156
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDA--------DGLEYLPPGARWLKAAGLEIPP-------GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284005078  157 DVKKNSHFSDFMDKQTGYVTRNLLAVPIVAGKEVLAVVMAVNKisAPEFSKQDEEVFSKYLSFVAVAL 224
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
72-241 2.68e-11

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 63.38  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  72 EAGSAEQMAHRALQRLAQLLQADCCSMFscrarngIPEVASRLLNVTPTSKFEDNLVapdREVVFPLDIGIVGWVAHVKK 151
Cdd:COG3605   15 SALDLDEALDRIVRRIAEALGVDVCSIY-------LLDPDGGRLELRATEGLNPEAV---GKVRLPLGEGLVGLVAERGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 152 ALNVSDVKKNSHFSDF-MDKQTGYvtRNLLAVPIVAGKEVLAvVMAVNKISAPEFSKQDEEVFSKYLSFVAVALrlqHTS 230
Cdd:COG3605   85 PLNLADAASHPRFKYFpETGEEGF--RSFLGVPIIRRGRVLG-VLVVQSREPREFTEEEVEFLVTLAAQLAEAI---ANA 158
                        170
                 ....*....|.
gi 284005078 231 YLYSVESRRSQ 241
Cdd:COG3605  159 ELLGELRAALA 169
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
560-732 2.46e-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: 56.15  E-value: 2.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   560 TYHNWRHGFNVGQTMFTLLMTGRLkkyytdLEAFAMLAAAFCHDIDHRGTNNLYQMKstsplarlhgTSILERHHLEYSK 639
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   640 TLLQDESLNIFQNlnkrqfetvihlfevaIIATDLALYFKKRTMfqkivdtceqmqseeetikyvtsDPTKKEVIMAMMM 719
Cdd:smart00471  66 ILLEEEEPRILEE----------------ILRTAILSHHERPDG-----------------------LRGEPITLEARIV 106
                          170
                   ....*....|...
gi 284005078   720 TACDLSAITKPWE 732
Cdd:smart00471 107 KVADRLDALRADR 119
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
561-736 3.57e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.42  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 561 YHNWRHGFNVGQTMFTLLMtgrlKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKStsplarlhgtSILERHHLEYSKT 640
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE----ELGLSEEDIELLRLAALLHDIGKPGTPDAITEEE----------SELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 641 LLQDEslnifqnlnkrQFETVIHLFEVAIIATDLALYFKkrtmfqkivdtceqmqseEETIKYVTSDPTKKEVIMAMMMT 720
Cdd:cd00077   67 ILREL-----------LLEEVIKLIDELILAVDASHHER------------------LDGLGYPDGLKGEEITLEARIVK 117
                        170
                 ....*....|....*.
gi 284005078 721 ACDLSAITKPWEVQSQ 736
Cdd:cd00077  118 LADRLDALRRDSREKR 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
256-433 1.66e-05

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 45.16  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  256 DVERQFHKALYTIRTYLNCDRYSIGLLDmtkekefydewpiklgevepykgpktPDGREIIfykiidyilhgkeeinvip 335
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD--------------------------ADGLEYL------------------- 35
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  336 sPPADHWTLVSGL------PTYVAENGFICNMLNAPADEYFTFQKGPVDETGwvIKNVLSLPIVNKKEdIVGVATFYNRK 409
Cdd:pfam01590  36 -PPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDDGE-LLGVLVLHHPR 111
                         170       180
                  ....*....|....*....|....
gi 284005078  410 DgkPFDEHDEHITETLTQFLGWSL 433
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
236-448 9.41e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 45.95  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 236 ESRRSQILMwSANKVFEELTDVERQFHKALYTIRTYLNCDRYSIGLLDmtkekefydewpiklgevepykgpktPDGREI 315
Cdd:COG2203  188 ELERLALLN-EISQALRSALDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGEL 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 316 IFYKIIDyilhgkeeinvIPSPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFT-FQKGPVDETGwvIKNVLSLPIVN 394
Cdd:COG2203  241 ELVAAPG-----------LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLV 307
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 284005078 395 KKEdIVGVATFYNRKDGkPFDEHDEHITETLTQFLGWSLLNTDTYERVNKLESR 448
Cdd:COG2203  308 DGR-LIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
561-780 1.97e-91

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.52  E-value: 1.97e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  561 YHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGT-SILERHHLEYSK 639
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  640 TLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDtceqmqsEEETIKYVTSDPTKKEVIMAMMM 719
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLE-------SKKTLDFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  720 TACDLSAITKPWEVQSQ------------------------PMMDRSKKDELPKLQVGFIDFVCTFVYKEFSRFHGEITP 775
Cdd:pfam00233 154 KAADISNPTRPWEISKKwadlvaeeffrqgdlekelglpvsPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQP 233

                  ....*
gi 284005078  776 MLNGL 780
Cdd:pfam00233 234 LLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
81-232 3.44e-22

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: 93.60  E-value: 3.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078    81 HRALQRLAQLLQADCCSMFSCRaRNGIPEVASRLLnvtptskfeDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVkk 160
Cdd:smart00065   7 QTILEELRQLLGADRVLIYLVD-ENDRGELVLVAA---------DGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDV-- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284005078   161 NSHFSDFMDKQTGY-VTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYL 232
Cdd:smart00065  75 EADPLFAEDLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
256-443 3.47e-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: 3.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   256 DVERQFHKALYTIRTYLNCDRYSIGLLDMtkekefydewpiklgevepykgpktpDGREIIFYKIIDYILhgkeeinviP 335
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDE--------------------------NDRGELVLVAADGLT---------L 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   336 SPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFtfqKGPVDETGWVIKNVLSLPIVNKKEdIVGVATFYNRKDGKPFD 415
Cdd:smart00065  46 PTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF---AEDLLGRYQGVRSFLAVPLVADGE-LVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 284005078   416 EHDEHITETLTQFLGWSLLNTDTYERVN 443
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
77-224 2.86e-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: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   77 EQMAHRALQRLAQLLQADCCSMFSCRArngipevaSRLLNVTPTSKFEDNLVAPDREvvfpldiGIVGWVAHVKKALNVS 156
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDA--------DGLEYLPPGARWLKAAGLEIPP-------GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284005078  157 DVKKNSHFSDFMDKQTGYVTRNLLAVPIVAGKEVLAVVMAVNKisAPEFSKQDEEVFSKYLSFVAVAL 224
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
72-241 2.68e-11

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 63.38  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  72 EAGSAEQMAHRALQRLAQLLQADCCSMFscrarngIPEVASRLLNVTPTSKFEDNLVapdREVVFPLDIGIVGWVAHVKK 151
Cdd:COG3605   15 SALDLDEALDRIVRRIAEALGVDVCSIY-------LLDPDGGRLELRATEGLNPEAV---GKVRLPLGEGLVGLVAERGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 152 ALNVSDVKKNSHFSDF-MDKQTGYvtRNLLAVPIVAGKEVLAvVMAVNKISAPEFSKQDEEVFSKYLSFVAVALrlqHTS 230
Cdd:COG3605   85 PLNLADAASHPRFKYFpETGEEGF--RSFLGVPIIRRGRVLG-VLVVQSREPREFTEEEVEFLVTLAAQLAEAI---ANA 158
                        170
                 ....*....|.
gi 284005078 231 YLYSVESRRSQ 241
Cdd:COG3605  159 ELLGELRAALA 169
GAF COG2203
GAF domain [Signal transduction mechanisms];
72-270 5.43e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 66.37  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  72 EAGSAEQMAHRALQRLAQLLQADCCSMFscrarngIPEVASRLLNVTPTSKFEDNLVAPdrevvFPLDIGIVGWVAHVKK 151
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAIL-------LVDEDGGELELVAAPGLPEEELGR-----LPLGEGLAGRALRTGE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 152 ALNVSDVKKNSHFSDFMDKQTG-YVTRNLLAVPIVAGKEVLAVVMAVNKiSAPEFSKQDEEVfskyLSFVA--VALRLQH 228
Cdd:COG2203  272 PVVVNDASTDPRFAPSLRELLLaLGIRSLLCVPLLVDGRLIGVLALYSK-EPRAFTEEDLEL----LEALAdqAAIAIER 346
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 284005078 229 tSYLYSVESRRSQILMWSANKVFEELTDVERQFHKALYTIRT 270
Cdd:COG2203  347 -ARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLEL 387
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
560-732 2.46e-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: 56.15  E-value: 2.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   560 TYHNWRHGFNVGQTMFTLLMTGRLkkyytdLEAFAMLAAAFCHDIDHRGTNNLYQMKstsplarlhgTSILERHHLEYSK 639
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   640 TLLQDESLNIFQNlnkrqfetvihlfevaIIATDLALYFKKRTMfqkivdtceqmqseeetikyvtsDPTKKEVIMAMMM 719
Cdd:smart00471  66 ILLEEEEPRILEE----------------ILRTAILSHHERPDG-----------------------LRGEPITLEARIV 106
                          170
                   ....*....|...
gi 284005078   720 TACDLSAITKPWE 732
Cdd:smart00471 107 KVADRLDALRADR 119
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
561-736 3.57e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.42  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 561 YHNWRHGFNVGQTMFTLLMtgrlKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKStsplarlhgtSILERHHLEYSKT 640
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAE----ELGLSEEDIELLRLAALLHDIGKPGTPDAITEEE----------SELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 641 LLQDEslnifqnlnkrQFETVIHLFEVAIIATDLALYFKkrtmfqkivdtceqmqseEETIKYVTSDPTKKEVIMAMMMT 720
Cdd:cd00077   67 ILREL-----------LLEEVIKLIDELILAVDASHHER------------------LDGLGYPDGLKGEEITLEARIVK 117
                        170
                 ....*....|....*.
gi 284005078 721 ACDLSAITKPWEVQSQ 736
Cdd:cd00077  118 LADRLDALRRDSREKR 133
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
256-433 1.66e-05

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 45.16  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  256 DVERQFHKALYTIRTYLNCDRYSIGLLDmtkekefydewpiklgevepykgpktPDGREIIfykiidyilhgkeeinvip 335
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD--------------------------ADGLEYL------------------- 35
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078  336 sPPADHWTLVSGL------PTYVAENGFICNMLNAPADEYFTFQKGPVDETGwvIKNVLSLPIVNKKEdIVGVATFYNRK 409
Cdd:pfam01590  36 -PPGARWLKAAGLeippgtGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIIDDGE-LLGVLVLHHPR 111
                         170       180
                  ....*....|....*....|....
gi 284005078  410 DgkPFDEHDEHITETLTQFLGWSL 433
Cdd:pfam01590 112 P--PFTEEELELLEVLADQVAIAL 133
GAF COG2203
GAF domain [Signal transduction mechanisms];
236-448 9.41e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 45.95  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 236 ESRRSQILMwSANKVFEELTDVERQFHKALYTIRTYLNCDRYSIGLLDmtkekefydewpiklgevepykgpktPDGREI 315
Cdd:COG2203  188 ELERLALLN-EISQALRSALDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGEL 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 316 IFYKIIDyilhgkeeinvIPSPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFT-FQKGPVDETGwvIKNVLSLPIVN 394
Cdd:COG2203  241 ELVAAPG-----------LPEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLV 307
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 284005078 395 KKEdIVGVATFYNRKDGkPFDEHDEHITETLTQFLGWSLLNTDTYERVNKLESR 448
Cdd:COG2203  308 DGR-LIGVLALYSKEPR-AFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
75-225 1.25e-04

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: 42.84  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078   75 SAEQMAHRALQRLAQLLQADCCSMfscrarnGIPEVASRLLNVTPTSKFEDNlvapdrEVVFPLDIGIVGWVAHVKKALN 154
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFI-------LLVDDDGRLAAWGGAADELSA------ALDDPPGEGLVGEALRTGRPVI 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284005078  155 VSDVKKNSHFSDFMDKQTGYvtRNLLAVPIVAGKEVLAvVMAVNKISAPEFSKQDEEVFSKYLSFVAVALR 225
Cdd:pfam13185  70 VNDLAADPAKKGLPAGHAGL--RSFLSVPLVSGGRVVG-VLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
347-454 7.59e-04

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284005078 347 GLPTYVAENGFICNMLNAPADEYFTFqkgpVDETG-WVIKNVLSLPIVNKKEdIVGVATFYNRKDgKPFDEHDEHITETL 425
Cdd:COG3605   74 GLVGLVAERGEPLNLADAASHPRFKY----FPETGeEGFRSFLGVPIIRRGR-VLGVLVVQSREP-REFTEEEVEFLVTL 147
                         90       100
                 ....*....|....*....|....*....
gi 284005078 426 TQFLGWSLLNTDTYERVNKLESRKDIAQE 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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