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Conserved domains on  [gi|170650674|ref|NP_000431|]
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rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha isoform 1 [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;
558-802 4.19e-104

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 4.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  558 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 636
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  637 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 716
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  717 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 796
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 170650674  797 PMLDGI 802
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
254-441 1.30e-23

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: 97.84  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   254 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 333
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   334 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 413
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 170650674   414 EMDETLMESLTQFLGWSVLNPDTYESMN 441
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
75-232 4.93e-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: 93.21  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674    75 EKCIFNVMKKLCFLLQADRMSLFMYrTRNGIAELATRLFNVHKDAVLEDClvmpdqeivFPLDMGIVGHVAHSKKIANVP 154
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLV-DENDRGELVLVAADGLTLPTLGIR---------FPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650674   155 NTEEDEHFCDfvDILTEY-KTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHN 232
Cdd:smart00065  73 DVEADPLFAE--DLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
558-802 4.19e-104

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 4.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  558 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 636
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  637 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 716
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  717 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 796
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 170650674  797 PMLDGI 802
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
254-441 1.30e-23

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: 97.84  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   254 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 333
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   334 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 413
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 170650674   414 EMDETLMESLTQFLGWSVLNPDTYESMN 441
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
75-232 4.93e-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: 93.21  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674    75 EKCIFNVMKKLCFLLQADRMSLFMYrTRNGIAELATRLFNVHKDAVLEDClvmpdqeivFPLDMGIVGHVAHSKKIANVP 154
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLV-DENDRGELVLVAADGLTLPTLGIR---------FPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650674   155 NTEEDEHFCDfvDILTEY-KTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHN 232
Cdd:smart00065  73 DVEADPLFAE--DLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
75-211 4.27e-11

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: 61.34  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   75 EKCIFNVMKKLCFLLQADRMSLFMYRtRNGIAelatrlfnvhkdaVLEDCLVMPDQEIVFPLDmGIVGHVAHSKKIANVP 154
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPD-ADGLE-------------YLPPGARWLKAAGLEIPP-GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 170650674  155 NTEEDEHFCDFVDILTEYKTKNILASPIMNGKDVVAIIMAVNKvdGSHFTKRDEEIL 211
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELL 122
GAF COG2203
GAF domain [Signal transduction mechanisms];
55-270 1.12e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 62.13  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  55 MEESEIIFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRlFNVHKDAVLEdclvmpdqeivF 134
Cdd:COG2203  189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAA-PGLPEEELGR-----------L 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 135 PLDMGIVGHVAHSKKIANVPNTEEDEHFCDF-VDILTEYKTKNILASPIMNGKDVVAIIMAVNKVDGsHFTKRDEEILlk 213
Cdd:COG2203  257 PLGEGLAGRALRTGEPVVVNDASTDPRFAPSlRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELL-- 333
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 170650674 214 yLNFANLIMKVYHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFL 270
Cdd:COG2203  334 -EALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLL 389
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
557-657 1.34e-08

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: 53.84  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   557 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 636
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 170650674   637 TLLRDESLNIFQNLNR---RQHEH 657
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
254-431 2.65e-07

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 50.56  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  254 DIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtpdgreinfYKVIDYILHGKEDIKVIP 333
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD----------------------------------ADGLEYLPPGARWLKAAG 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  334 NPPPDhwalvsGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFD 413
Cdd:pfam01590  47 LEIPP------GTGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFT 115
                         170
                  ....*....|....*...
gi 170650674  414 EMDETLMESLTQFLGWSV 431
Cdd:pfam01590 116 EEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
558-743 7.56e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 49.26  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 558 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 637
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 638 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 717
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 170650674 718 ACDLSAITK--PWEVQSQVALLVAAEFW 743
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
253-446 3.52e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.96  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 253 TDIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtPDGREINFYKVIDyilhgkedikvI 332
Cdd:COG2203  206 LDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGELELVAAPG-----------L 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 333 PNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFA-FQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkP 411
Cdd:COG2203  249 PEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-A 324
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 170650674 412 FDEMDETLMESLTQFLGWSVLNPDTYESMNKLENR 446
Cdd:COG2203  325 FTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
558-802 4.19e-104

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 321.42  E-value: 4.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  558 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 636
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  637 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 716
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  717 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 796
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 170650674  797 PMLDGI 802
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
254-441 1.30e-23

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: 97.84  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   254 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 333
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   334 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 413
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 170650674   414 EMDETLMESLTQFLGWSVLNPDTYESMN 441
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
75-232 4.93e-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: 93.21  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674    75 EKCIFNVMKKLCFLLQADRMSLFMYrTRNGIAELATRLFNVHKDAVLEDClvmpdqeivFPLDMGIVGHVAHSKKIANVP 154
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLV-DENDRGELVLVAADGLTLPTLGIR---------FPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650674   155 NTEEDEHFCDfvDILTEY-KTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHN 232
Cdd:smart00065  73 DVEADPLFAE--DLLGRYqGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
75-211 4.27e-11

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: 61.34  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   75 EKCIFNVMKKLCFLLQADRMSLFMYRtRNGIAelatrlfnvhkdaVLEDCLVMPDQEIVFPLDmGIVGHVAHSKKIANVP 154
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPD-ADGLE-------------YLPPGARWLKAAGLEIPP-GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 170650674  155 NTEEDEHFCDFVDILTEYKTKNILASPIMNGKDVVAIIMAVNKvdGSHFTKRDEEIL 211
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP--RPPFTEEELELL 122
GAF COG2203
GAF domain [Signal transduction mechanisms];
55-270 1.12e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 62.13  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  55 MEESEIIFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRlFNVHKDAVLEdclvmpdqeivF 134
Cdd:COG2203  189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAA-PGLPEEELGR-----------L 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 135 PLDMGIVGHVAHSKKIANVPNTEEDEHFCDF-VDILTEYKTKNILASPIMNGKDVVAIIMAVNKVDGsHFTKRDEEILlk 213
Cdd:COG2203  257 PLGEGLAGRALRTGEPVVVNDASTDPRFAPSlRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPR-AFTEEDLELL-- 333
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 170650674 214 yLNFANLIMKVYHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFL 270
Cdd:COG2203  334 -EALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLL 389
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
557-657 1.34e-08

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: 53.84  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674   557 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 636
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 170650674   637 TLLRDESLNIFQNLNR---RQHEH 657
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
254-431 2.65e-07

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 50.56  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  254 DIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtpdgreinfYKVIDYILHGKEDIKVIP 333
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD----------------------------------ADGLEYLPPGARWLKAAG 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  334 NPPPDhwalvsGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFD 413
Cdd:pfam01590  47 LEIPP------GTGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFT 115
                         170
                  ....*....|....*...
gi 170650674  414 EMDETLMESLTQFLGWSV 431
Cdd:pfam01590 116 EEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
558-743 7.56e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 49.26  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 558 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 637
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 638 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 717
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 170650674 718 ACDLSAITK--PWEVQSQVALLVAAEFW 743
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
253-446 3.52e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.96  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 253 TDIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtPDGREINFYKVIDyilhgkedikvI 332
Cdd:COG2203  206 LDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGELELVAAPG-----------L 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674 333 PNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFA-FQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkP 411
Cdd:COG2203  249 PEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-A 324
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 170650674 412 FDEMDETLMESLTQFLGWSVLNPDTYESMNKLENR 446
Cdd:COG2203  325 FTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
66-211 4.69e-05

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  66 RDFQENLQTekcifnVMKKLCFLLQADRMSLFMYRTRNGIAEL-ATRlfNVHKDAVledclvmpdQEIVFPLDMGIVGHV 144
Cdd:COG3605   17 LDLDEALDR------IVRRIAEALGVDVCSIYLLDPDGGRLELrATE--GLNPEAV---------GKVRLPLGEGLVGLV 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650674 145 AHSKKIANVPNTEEDEHFcDFVDILTEYKTKNILASPIMNGKDVVAIImAVNKVDGSHFTKRDEEIL 211
Cdd:COG3605   80 AERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPIIRRGRVLGVL-VVQSREPREFTEEEVEFL 144
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
130-211 6.75e-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: 37.83  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650674  130 QEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTknILASPIMNGKDVVAIImAVNKVDGSHFTKRDEE 209
Cdd:pfam13185  47 AALDDPPGEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGLRS--FLSVPLVSGGRVVGVL-ALGSNRPGAFDEEDLE 123

                  ..
gi 170650674  210 IL 211
Cdd:pfam13185 124 LL 125
 
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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