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Conserved domains on  [gi|1622941262|ref|XP_001099553|]
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cGMP-specific 3',5'-cyclic phosphodiesterase isoform X2 [Macaca mulatta]

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;
570-804 9.30e-108

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 330.28  E-value: 9.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 570 YHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCH-SIMEHHHFDQCL 648
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 649 MILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQ---FNLEDPHQKELFLAMLMTACDLSA 725
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622941262 726 ITKPWPIQQRIAELVASEFFDQGDRErKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC 804
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLE-KELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
122-279 9.74e-29

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: 112.47  E-value: 9.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  122 DVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDkfLISRLFDVAEGSTLEeasnncIRLEWNKGIVGHVAALGEPLNIK 201
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE--LVLVAADGLTLPTLG------IRFPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941262  202 DAYEDPRFNAEVDQITGyKTQSILCMPIKNHrEEVVGVAQAINKKSgnGGTFTEKDEKDFAAYLAFCGIVLHNAQLYE 279
Cdd:smart00065  73 DVEADPLFAEDLLGRYQ-GVRSFLAVPLVAD-GELVGVLALHNKKS--PRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
305-471 1.84e-24

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: 100.15  E-value: 1.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  305 LEVILKKIAATIISFMQVQKCTIFIVDEDCsdsfssvfHMECEELEKSSDMLTREHDANKINYMYAQYVKNTMEPLNIPD 384
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDEND--------RGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  385 VSKDkRFPWTTENTGNvsqQCIRSLLCTPIKNGkkNKVIGVCQLVNKmeentGKVKPFNRNDEQFLEAFVIFCGLGIQNT 464
Cdd:smart00065  74 VEAD-PLFAEDLLGRY---QGVRSFLAVPLVAD--GELVGVLALHNK-----KSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 1622941262  465 QMYEAVE 471
Cdd:smart00065 143 QLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
570-804 9.30e-108

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 330.28  E-value: 9.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 570 YHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCH-SIMEHHHFDQCL 648
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 649 MILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQ---FNLEDPHQKELFLAMLMTACDLSA 725
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622941262 726 ITKPWPIQQRIAELVASEFFDQGDRErKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC 804
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLE-KELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
122-279 9.74e-29

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: 112.47  E-value: 9.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  122 DVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDkfLISRLFDVAEGSTLEeasnncIRLEWNKGIVGHVAALGEPLNIK 201
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE--LVLVAADGLTLPTLG------IRFPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941262  202 DAYEDPRFNAEVDQITGyKTQSILCMPIKNHrEEVVGVAQAINKKSgnGGTFTEKDEKDFAAYLAFCGIVLHNAQLYE 279
Cdd:smart00065  73 DVEADPLFAEDLLGRYQ-GVRSFLAVPLVAD-GELVGVLALHNKKS--PRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
305-471 1.84e-24

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: 100.15  E-value: 1.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  305 LEVILKKIAATIISFMQVQKCTIFIVDEDCsdsfssvfHMECEELEKSSDMLTREHDANKINYMYAQYVKNTMEPLNIPD 384
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDEND--------RGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  385 VSKDkRFPWTTENTGNvsqQCIRSLLCTPIKNGkkNKVIGVCQLVNKmeentGKVKPFNRNDEQFLEAFVIFCGLGIQNT 464
Cdd:smart00065  74 VEAD-PLFAEDLLGRY---QGVRSFLAVPLVAD--GELVGVLALHNK-----KSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 1622941262  465 QMYEAVE 471
Cdd:smart00065 143 QLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
108-309 4.59e-19

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 85.72  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 108 SRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSndkflisRLFDVA-EGSTLEEASNncIRLEWNKG 186
Cdd:COG3605     4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGG-------RLELRAtEGLNPEAVGK--VRLPLGEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 187 IVGHVAALGEPLNIKDAYEDPRFnAEVDQITGYKTQSILCMPIKnHREEVVGVAQAINKKSgngGTFTEkDEKDF----A 262
Cdd:COG3605    75 LVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSREP---REFTE-EEVEFlvtlA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622941262 263 AYLAfcgIVLHNAQLYETSLLENKRNQVLLDLaslifEEQQSLEVIL 309
Cdd:COG3605   149 AQLA---EAIANAELLGELRAALAELSLAREE-----EREAAVEAAI 187
GAF COG2203
GAF domain [Signal transduction mechanisms];
279-528 9.16e-15

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 78.31  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 279 ETSLLENKRNQVLLDLASLIFEEQqSLEVILKKIAATIISFMQVQKCTIFIVDEDCSD-SFSSVFHMECEELEKssdmLT 357
Cdd:COG2203   183 QRARLELERLALLNEISQALRSAL-DLEELLQRILELAGELLGADRGAILLVDEDGGElELVAAPGLPEEELGR----LP 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 358 REHDankinymYAQYVKNTMEPLNIPDVSKDKRfpWTTENTGNVSQQCIRSLLCTPIKNGkkNKVIGVCQLVNKmeentg 437
Cdd:COG2203   258 LGEG-------LAGRALRTGEPVVVNDASTDPR--FAPSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSK------ 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 438 KVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDF 517
Cdd:COG2203   321 EPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGA 400
                         250
                  ....*....|.
gi 1622941262 518 SFSDFELSDLE 528
Cdd:COG2203   401 ELLLLLLDAAD 411
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
570-745 5.66e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 66.98  E-value: 5.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 570 YHNWRHAFNTAQCMFAALKAgkiqNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSehplaqlychSIMEHHHFDQCLM 649
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEE----LGLSEEDIELLRLAALLHDIGKPGTPDAITEEE----------SELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 650 ILNSpgnqilsglsiEEYKTTLKIIKQAILATDLalyikrrgEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITK- 728
Cdd:cd00077    67 ILRE-----------LLLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRr 127
                         170
                  ....*....|....*...
gi 1622941262 729 -PWPIQQRIAELVASEFF 745
Cdd:cd00077   128 dSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
304-461 7.87e-13

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: 66.35  E-value: 7.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 304 SLEVILKKIAATIISFMQVQKCTIFIVDEDcsdsfssvfhmECEELEKSSDMLTREHDANKINYMyaQYVKNTMEPLNIP 383
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDAD-----------GLEYLPPGARWLKAAGLEIPPGTG--VTVLRTGRPLVVP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941262 384 DVSKDKRFPwttENTGNVSQQCIRSLLCTPIKNGkkNKVIGVCQLVNkmeentgKVKPFNRNDEQFLEAFVIFCGLGI 461
Cdd:pfam01590  68 DAAGDPRFL---DPLLLLRNFGIRSLLAVPIIDD--GELLGVLVLHH-------PRPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
569-736 8.02e-13

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: 65.78  E-value: 8.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  569 AYHNWRHAFNTAQCmfaalkAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEhplaqlychsIMEHHHFDQCL 648
Cdd:smart00471   2 DYHVFEHSLRVAQL------AAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKTS----------VLEDHHFIGAE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  649 MILNSPGNQILsglsieeykttLKIIKQAILAtdlalyikrrgeffeliRKNQFNLEdPHQKELFLAMLMTACDLSAITK 728
Cdd:smart00471  66 ILLEEEEPRIL-----------EEILRTAILS-----------------HHERPDGL-RGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 1622941262  729 PWPIQQRI 736
Cdd:smart00471 117 ADRRYRRV 124
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
122-272 2.03e-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: 62.11  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 122 DVTALCHKIFLHIHGLISADRYSLFLVCEDssndkflisRLFDVAEGSTLEEASNNCIRLewnkGIVGHVAALGEPLNIK 201
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDAD---------GLEYLPPGARWLKAAGLEIPP----GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622941262 202 DAYEDPRFNAEVDQITGYKTQSILCMPIKNHrEEVVGVAQAINKKSGnggtFTEKDEKDFAAYLAFCGIVL 272
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHPRPP----FTEEELELLEVLADQVAIAL 133
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
171-239 1.31e-03

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 42.29  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622941262 171 LEEASNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAeVDQITGYKTQSILCMPIKnHREEVVGV 239
Cdd:PRK11061   58 LKKPRGRTVTLAFDEGIVGLVGRLAEPINLADAQKHPSFKY-IPSVKEERFRAFLGVPII-YRRQLLGV 124
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
570-804 9.30e-108

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 330.28  E-value: 9.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 570 YHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCH-SIMEHHHFDQCL 648
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 649 MILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQ---FNLEDPHQKELFLAMLMTACDLSA 725
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKtldFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622941262 726 ITKPWPIQQRIAELVASEFFDQGDRErKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC 804
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLE-KELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
122-279 9.74e-29

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: 112.47  E-value: 9.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  122 DVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDkfLISRLFDVAEGSTLEeasnncIRLEWNKGIVGHVAALGEPLNIK 201
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE--LVLVAADGLTLPTLG------IRFPLDEGLAGRVAETGRPLNIP 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941262  202 DAYEDPRFNAEVDQITGyKTQSILCMPIKNHrEEVVGVAQAINKKSgnGGTFTEKDEKDFAAYLAFCGIVLHNAQLYE 279
Cdd:smart00065  73 DVEADPLFAEDLLGRYQ-GVRSFLAVPLVAD-GELVGVLALHNKKS--PRPFTEEDEELLQALANQLAIALANAQLYE 146
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
305-471 1.84e-24

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: 100.15  E-value: 1.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  305 LEVILKKIAATIISFMQVQKCTIFIVDEDCsdsfssvfHMECEELEKSSDMLTREHDANKINYMYAQYVKNTMEPLNIPD 384
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDEND--------RGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  385 VSKDkRFPWTTENTGNvsqQCIRSLLCTPIKNGkkNKVIGVCQLVNKmeentGKVKPFNRNDEQFLEAFVIFCGLGIQNT 464
Cdd:smart00065  74 VEAD-PLFAEDLLGRY---QGVRSFLAVPLVAD--GELVGVLALHNK-----KSPRPFTEEDEELLQALANQLAIALANA 142

                   ....*..
gi 1622941262  465 QMYEAVE 471
Cdd:smart00065 143 QLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
108-309 4.59e-19

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 85.72  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 108 SRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSndkflisRLFDVA-EGSTLEEASNncIRLEWNKG 186
Cdd:COG3605     4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGG-------RLELRAtEGLNPEAVGK--VRLPLGEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 187 IVGHVAALGEPLNIKDAYEDPRFnAEVDQITGYKTQSILCMPIKnHREEVVGVAQAINKKSgngGTFTEkDEKDF----A 262
Cdd:COG3605    75 LVGLVAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPII-RRGRVLGVLVVQSREP---REFTE-EEVEFlvtlA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622941262 263 AYLAfcgIVLHNAQLYETSLLENKRNQVLLDLaslifEEQQSLEVIL 309
Cdd:COG3605   149 AQLA---EAIANAELLGELRAALAELSLAREE-----EREAAVEAAI 187
GAF COG2203
GAF domain [Signal transduction mechanisms];
110-309 3.76e-17

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 86.02  E-value: 3.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 110 LLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSndkflisRLFDVAEGSTLEEAsnnCIRLEWNKGIVG 189
Cdd:COG2203   195 LNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGG-------ELELVAAPGLPEEE---LGRLPLGEGLAG 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 190 HVAALGEPLNIKDAYEDPRF-NAEVDQITGYKTQSILCMPIKnHREEVVGVAQAINKKSgngGTFTEkDEKDFAAYLAF- 267
Cdd:COG2203   265 RALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEP---RAFTE-EDLELLEALADq 339
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622941262 268 CGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVIL 309
Cdd:COG2203   340 AAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLR 381
GAF COG2203
GAF domain [Signal transduction mechanisms];
279-528 9.16e-15

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 78.31  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 279 ETSLLENKRNQVLLDLASLIFEEQqSLEVILKKIAATIISFMQVQKCTIFIVDEDCSD-SFSSVFHMECEELEKssdmLT 357
Cdd:COG2203   183 QRARLELERLALLNEISQALRSAL-DLEELLQRILELAGELLGADRGAILLVDEDGGElELVAAPGLPEEELGR----LP 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 358 REHDankinymYAQYVKNTMEPLNIPDVSKDKRfpWTTENTGNVSQQCIRSLLCTPIKNGkkNKVIGVCQLVNKmeentg 437
Cdd:COG2203   258 LGEG-------LAGRALRTGEPVVVNDASTDPR--FAPSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSK------ 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 438 KVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDF 517
Cdd:COG2203   321 EPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGA 400
                         250
                  ....*....|.
gi 1622941262 518 SFSDFELSDLE 528
Cdd:COG2203   401 ELLLLLLDAAD 411
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
570-745 5.66e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 66.98  E-value: 5.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 570 YHNWRHAFNTAQCMFAALKAgkiqNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSehplaqlychSIMEHHHFDQCLM 649
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEE----LGLSEEDIELLRLAALLHDIGKPGTPDAITEEE----------SELEKDHAIVGAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 650 ILNSpgnqilsglsiEEYKTTLKIIKQAILATDLalyikrrgEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITK- 728
Cdd:cd00077    67 ILRE-----------LLLEEVIKLIDELILAVDA--------SHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRr 127
                         170
                  ....*....|....*...
gi 1622941262 729 -PWPIQQRIAELVASEFF 745
Cdd:cd00077   128 dSREKRRRIAEEDLEELL 145
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
304-461 7.87e-13

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: 66.35  E-value: 7.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 304 SLEVILKKIAATIISFMQVQKCTIFIVDEDcsdsfssvfhmECEELEKSSDMLTREHDANKINYMyaQYVKNTMEPLNIP 383
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDAD-----------GLEYLPPGARWLKAAGLEIPPGTG--VTVLRTGRPLVVP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941262 384 DVSKDKRFPwttENTGNVSQQCIRSLLCTPIKNGkkNKVIGVCQLVNkmeentgKVKPFNRNDEQFLEAFVIFCGLGI 461
Cdd:pfam01590  68 DAAGDPRFL---DPLLLLRNFGIRSLLAVPIIDD--GELLGVLVLHH-------PRPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
569-736 8.02e-13

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: 65.78  E-value: 8.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  569 AYHNWRHAFNTAQCmfaalkAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEhplaqlychsIMEHHHFDQCL 648
Cdd:smart00471   2 DYHVFEHSLRVAQL------AAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKTS----------VLEDHHFIGAE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262  649 MILNSPGNQILsglsieeykttLKIIKQAILAtdlalyikrrgeffeliRKNQFNLEdPHQKELFLAMLMTACDLSAITK 728
Cdd:smart00471  66 ILLEEEEPRIL-----------EEILRTAILS-----------------HHERPDGL-RGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 1622941262  729 PWPIQQRI 736
Cdd:smart00471 117 ADRRYRRV 124
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
122-272 2.03e-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: 62.11  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 122 DVTALCHKIFLHIHGLISADRYSLFLVCEDssndkflisRLFDVAEGSTLEEASNNCIRLewnkGIVGHVAALGEPLNIK 201
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDAD---------GLEYLPPGARWLKAAGLEIPP----GTGVTVLRTGRPLVVP 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622941262 202 DAYEDPRFNAEVDQITGYKTQSILCMPIKNHrEEVVGVAQAINKKSGnggtFTEKDEKDFAAYLAFCGIVL 272
Cdd:pfam01590  68 DAAGDPRFLDPLLLLRNFGIRSLLAVPIIDD-GELLGVLVLHHPRPP----FTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
289-506 2.10e-10

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 60.68  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 289 QVLLDLASLIfEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDcsdsfssvfhmeceeleksSDMLtrehdankinYM 368
Cdd:COG3605     4 KALRRISEAV-ASALDLDEALDRIVRRIAEALGVDVCSIYLLDPD-------------------GGRL----------EL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 369 YA------QYVKN---------------TMEPLNIPDVSKDKRF---PWTTENTgnvsqqcIRSLLCTPIKNGkkNKVIG 424
Cdd:COG3605    54 RAteglnpEAVGKvrlplgeglvglvaeRGEPLNLADAASHPRFkyfPETGEEG-------FRSFLGVPIIRR--GRVLG 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 425 VcqLV--NKmeentgKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAkqmvtlevlsyHASAAEEETRElQSLA 502
Cdd:COG3605   125 V--LVvqSR------EPREFTEEEVEFLVTLAAQLAEAIANAELLGELRAALA-----------ELSLAREEERE-AAVE 184

                  ....
gi 1622941262 503 AAVV 506
Cdd:COG3605   185 AAIL 188
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
178-266 1.51e-05

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


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 45.97  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 178 CIRLEWNKGIVGHVAALGEPLNIKDAYEDPrfnaevdqitGY-----KTQSILCMPIKNHrEEVVGVaqaINKKSGNGGT 252
Cdd:COG1956    69 CTRIPFGKGVCGTAAAEGETQLVPDVHAFP----------GHiacdsASRSEIVVPIFKD-GEVIGV---LDIDSPTPGR 134
                          90
                  ....*....|....*..
gi 1622941262 253 FTEKDEK---DFAAYLA 266
Cdd:COG1956   135 FDEEDQAgleALAALLA 151
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
164-273 9.29e-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: 40.14  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941262 164 DVAEGSTLEEASNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKtqSILCMPIKnHREEVVGVaqaI 243
Cdd:pfam13185  34 RLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGLR--SFLSVPLV-SGGRVVGV---L 107
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622941262 244 NKKSGNGGTFTEKDEkDFAAYLAF-CGIVLH 273
Cdd:pfam13185 108 ALGSNRPGAFDEEDL-ELLELLAEqAAIAIE 137
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
171-239 1.31e-03

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 42.29  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622941262 171 LEEASNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAeVDQITGYKTQSILCMPIKnHREEVVGV 239
Cdd:PRK11061   58 LKKPRGRTVTLAFDEGIVGLVGRLAEPINLADAQKHPSFKY-IPSVKEERFRAFLGVPII-YRRQLLGV 124
 
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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