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Conserved domains on  [gi|514696300|ref|XP_004995720|]
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uncharacterized protein PTSG_11971 [Salpingoeca rosetta]

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;
364-596 1.26e-100

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 306.78  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  364 YHNWKHAFNVGQFVYGALMSSEMGTYFSDLEKAGILIAALSHDLDHRGTNNTFEKKYSTPLGDLYST-STLEHHHFDRAV 442
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  443 TILSTEGQNILAALPSKQYEQAIKQIESAILATDLGRHFSIRKEYKALVDDK---TFDKAKREHLDILRSIIMTAGDLSA 519
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300  520 VTKPFPAQRRVAELVYSEFFDQGDLERALGAKtddLQDLMNRQKVSELPKMQVGFIDFVAKPVYDSLGDHFEDLKVL 596
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLP---VSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPL 234
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
114-269 1.22e-27

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: 108.62  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   114 DTKEVVETILQHAAELVHCDRCSLFLYD-KETNELSSQAFDVSEEGCVGDSddnqfsFPATTGIAGHVATTGETLNIHDA 192
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDeNDRGELVLVAADGLTLPTLGIR------FPLDEGLAGRVAETGRPLNIPDV 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300   193 YADDRFNRAIDDKTGFkTRNILCTPIFdNNDEVIAVTQLINKHGDGPFTERDVKSLNVFAGYCGLALHNAQLHDQVR 269
Cdd:smart00065  75 EADPLFAEDLLGRYQG-VRSFLAVPLV-ADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
364-596 1.26e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 306.78  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  364 YHNWKHAFNVGQFVYGALMSSEMGTYFSDLEKAGILIAALSHDLDHRGTNNTFEKKYSTPLGDLYST-STLEHHHFDRAV 442
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  443 TILSTEGQNILAALPSKQYEQAIKQIESAILATDLGRHFSIRKEYKALVDDK---TFDKAKREHLDILRSIIMTAGDLSA 519
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300  520 VTKPFPAQRRVAELVYSEFFDQGDLERALGAKtddLQDLMNRQKVSELPKMQVGFIDFVAKPVYDSLGDHFEDLKVL 596
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLP---VSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPL 234
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
114-269 1.22e-27

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: 108.62  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   114 DTKEVVETILQHAAELVHCDRCSLFLYD-KETNELSSQAFDVSEEGCVGDSddnqfsFPATTGIAGHVATTGETLNIHDA 192
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDeNDRGELVLVAADGLTLPTLGIR------FPLDEGLAGRVAETGRPLNIPDV 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300   193 YADDRFNRAIDDKTGFkTRNILCTPIFdNNDEVIAVTQLINKHGDGPFTERDVKSLNVFAGYCGLALHNAQLHDQVR 269
Cdd:smart00065  75 EADPLFAEDLLGRYQG-VRSFLAVPLV-ADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
100-280 1.62e-22

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 95.35  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 100 TVMLDISAALMETTDTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAFDVSEEGCVGdsddnQFSFPATTGIAGH 179
Cdd:COG3605    4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVG-----KVRLPLGEGLVGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 180 VATTGETLNIHDAYADDRFNRAidDKTG-FKTRNILCTPIFDnNDEVIAVTQLINKhGDGPFTERDVKSLNVFAGYCGLA 258
Cdd:COG3605   79 VAERGEPLNLADAASHPRFKYF--PETGeEGFRSFLGVPIIR-RGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEA 154
                        170       180
                 ....*....|....*....|..
gi 514696300 259 LHNAQLHDQVRRDARRHQVALE 280
Cdd:COG3605  155 IANAELLGELRAALAELSLARE 176
GAF COG2203
GAF domain [Signal transduction mechanisms];
84-614 9.01e-22

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 100.27  E-value: 9.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  84 TVAEALRELALAQKFSTVMLDISAALMETTDTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAfdvseegCVGDS 163
Cdd:COG2203  177 IARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVA-------APGLP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 164 DDNQFSFPATTGIAGHVATTGETLNIHDAYADDRFNRAIDD-KTGFKTRNILCTPIFdNNDEVIAVTQLINKHgDGPFTE 242
Cdd:COG2203  250 EEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRElLLALGIRSLLCVPLL-VDGRLIGVLALYSKE-PRAFTE 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 243 RDVKSLNVFAGYCGLALHNAQLHDQvrRDARRHQVALEMLSYHTRAHPQEVEKLSTTEPPQELCTRLRSITFDPLSIDID 322
Cdd:COG2203  328 EDLELLEALADQAAIAIERARLYEA--LEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 323 DTLLAARAMFTDSGFARKLRMRPDDLSSWLICVKRSYRDVRYHNWKHAFNVGQFVYGALMSSEMGTYFSDLEKAGILIAA 402
Cdd:COG2203  406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 403 LSHDLDHRGTNNTFEKKYSTPLGDLYSTSTLEHHHFDRAVTILSTEGQNILAALPSKQYEQAIKQIESAILATDLGRHFS 482
Cdd:COG2203  486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 483 IRKEYKALVDDKTFDKAKREHLDILRSIIMTAGDLSAVTKPFPAQRRVAELVYSEFFDQGDLERALGAKTDDLQDLMNRQ 562
Cdd:COG2203  566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514696300 563 KVSELPKMQVGFIDFVAKPVYDSLGDHFEDLKVLRAEVERNRRDWEAMRDKG 614
Cdd:COG2203  646 LALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGL 697
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
114-259 2.52e-18

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 81.76  E-value: 2.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  114 DTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAFDVSEEGCVGDSDdnqfsfpattGIAGHVATTGETLNIHDAY 193
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP----------GTGVTVLRTGRPLVVPDAA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514696300  194 ADDRFNRAIDDKTGFKTRNILCTPIFDnNDEVIAVTQLINKhgDGPFTERDVKSLNVFAGYCGLAL 259
Cdd:pfam01590  71 GDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
364-530 1.09e-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: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   364 YHNWKHAFNVGQFVYgalmssEMGTYFSDLEKAGILIAALSHDLDHRGTNNTFEKKystplgdlysTSTLEHHHFDRAVT 443
Cdd:smart00471   3 YHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   444 ILSTEGQNILAalpskqyeqaikqiesAILATDLGRHFSIRKEYkalvddktfdkakREHLDILRSIIMTAGDLSAVTKP 523
Cdd:smart00471  67 LLEEEEPRILE----------------EILRTAILSHHERPDGL-------------RGEPITLEARIVKVADRLDALRA 117

                   ....*..
gi 514696300   524 FPAQRRV 530
Cdd:smart00471 118 DRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
364-539 1.42e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.88  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 364 YHNWKHAFNVGQFVygALMSSEMGTYFSDLEKagILIAALSHDLDHRGTNNTFekkystplgdLYSTSTLEHHHFDRAVT 443
Cdd:cd00077    1 EHRFEHSLRVAQLA--RRLAEELGLSEEDIEL--LRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 444 ILStegqnilaalpSKQYEQAIKQIESAILATDLgRHFSIRKEYKALVDDKtfdkakrEHLDILRSIIMTAGDLSAVTK- 522
Cdd:cd00077   67 ILR-----------ELLLEEVIKLIDELILAVDA-SHHERLDGLGYPDGLK-------GEEITLEARIVKLADRLDALRr 127
                        170
                 ....*....|....*...
gi 514696300 523 -PFPAQRRVAELVYSEFF 539
Cdd:cd00077  128 dSREKRRRIAEEDLEELL 145
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
364-596 1.26e-100

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 306.78  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  364 YHNWKHAFNVGQFVYGALMSSEMGTYFSDLEKAGILIAALSHDLDHRGTNNTFEKKYSTPLGDLYST-STLEHHHFDRAV 442
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDsSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  443 TILSTEGQNILAALPSKQYEQAIKQIESAILATDLGRHFSIRKEYKALVDDK---TFDKAKREHLDILRSIIMTAGDLSA 519
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300  520 VTKPFPAQRRVAELVYSEFFDQGDLERALGAKtddLQDLMNRQKVSELPKMQVGFIDFVAKPVYDSLGDHFEDLKVL 596
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLP---VSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPL 234
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
114-269 1.22e-27

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: 108.62  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   114 DTKEVVETILQHAAELVHCDRCSLFLYD-KETNELSSQAFDVSEEGCVGDSddnqfsFPATTGIAGHVATTGETLNIHDA 192
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDeNDRGELVLVAADGLTLPTLGIR------FPLDEGLAGRVAETGRPLNIPDV 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514696300   193 YADDRFNRAIDDKTGFkTRNILCTPIFdNNDEVIAVTQLINKHGDGPFTERDVKSLNVFAGYCGLALHNAQLHDQVR 269
Cdd:smart00065  75 EADPLFAEDLLGRYQG-VRSFLAVPLV-ADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
100-280 1.62e-22

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 95.35  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 100 TVMLDISAALMETTDTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAFDVSEEGCVGdsddnQFSFPATTGIAGH 179
Cdd:COG3605    4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVG-----KVRLPLGEGLVGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 180 VATTGETLNIHDAYADDRFNRAidDKTG-FKTRNILCTPIFDnNDEVIAVTQLINKhGDGPFTERDVKSLNVFAGYCGLA 258
Cdd:COG3605   79 VAERGEPLNLADAASHPRFKYF--PETGeEGFRSFLGVPIIR-RGRVLGVLVVQSR-EPREFTEEEVEFLVTLAAQLAEA 154
                        170       180
                 ....*....|....*....|..
gi 514696300 259 LHNAQLHDQVRRDARRHQVALE 280
Cdd:COG3605  155 IANAELLGELRAALAELSLARE 176
GAF COG2203
GAF domain [Signal transduction mechanisms];
84-614 9.01e-22

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 100.27  E-value: 9.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  84 TVAEALRELALAQKFSTVMLDISAALMETTDTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAfdvseegCVGDS 163
Cdd:COG2203  177 IARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVA-------APGLP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 164 DDNQFSFPATTGIAGHVATTGETLNIHDAYADDRFNRAIDD-KTGFKTRNILCTPIFdNNDEVIAVTQLINKHgDGPFTE 242
Cdd:COG2203  250 EEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRElLLALGIRSLLCVPLL-VDGRLIGVLALYSKE-PRAFTE 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 243 RDVKSLNVFAGYCGLALHNAQLHDQvrRDARRHQVALEMLSYHTRAHPQEVEKLSTTEPPQELCTRLRSITFDPLSIDID 322
Cdd:COG2203  328 EDLELLEALADQAAIAIERARLYEA--LEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 323 DTLLAARAMFTDSGFARKLRMRPDDLSSWLICVKRSYRDVRYHNWKHAFNVGQFVYGALMSSEMGTYFSDLEKAGILIAA 402
Cdd:COG2203  406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 403 LSHDLDHRGTNNTFEKKYSTPLGDLYSTSTLEHHHFDRAVTILSTEGQNILAALPSKQYEQAIKQIESAILATDLGRHFS 482
Cdd:COG2203  486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 483 IRKEYKALVDDKTFDKAKREHLDILRSIIMTAGDLSAVTKPFPAQRRVAELVYSEFFDQGDLERALGAKTDDLQDLMNRQ 562
Cdd:COG2203  566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514696300 563 KVSELPKMQVGFIDFVAKPVYDSLGDHFEDLKVLRAEVERNRRDWEAMRDKG 614
Cdd:COG2203  646 LALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGL 697
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
114-259 2.52e-18

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 81.76  E-value: 2.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  114 DTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAFDVSEEGCVGDSDdnqfsfpattGIAGHVATTGETLNIHDAY 193
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP----------GTGVTVLRTGRPLVVPDAA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514696300  194 ADDRFNRAIDDKTGFKTRNILCTPIFDnNDEVIAVTQLINKhgDGPFTERDVKSLNVFAGYCGLAL 259
Cdd:pfam01590  71 GDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
112-260 9.33e-12

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 62.87  E-value: 9.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  112 TTDTKEVVETILQHAAELVHCDRCSLFLYDKETNELSSqafdvseeGCVGDSDDNQFSFPATTGIAGHVATTGETLNIHD 191
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAW--------GGAADELSAALDDPPGEGLVGEALRTGRPVIVND 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514696300  192 AYADDRFNRAIDDKTGFktRNILCTPIFDNNdEVIAVTQLINkHGDGPFTERDVKSLNVFAGYCGLALH 260
Cdd:pfam13185  73 LAADPAKKGLPAGHAGL--RSFLSVPLVSGG-RVVGVLALGS-NRPGAFDEEDLELLELLAEQAAIAIE 137
GAF_3 pfam13492
GAF domain;
116-261 1.02e-08

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 53.91  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  116 KEVVETILQHAAELVHCDRCSLFLYDKETNELSSQAfdvseeGCVGdSDDNQFSFPATTGIAGHVATTGETLNIhdayad 195
Cdd:pfam13492   3 DEILEALLKLLVRLLGAERAAVYLLDEDGNKLQVAA------GYDG-EPDPSESLDADSPLARRALSSGEPISG------ 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514696300  196 drfnRAIDDKTGFKTRNILCTPIFDnNDEVIAVTqLINKHGDGPFTERDVKSLNVFAGYCGLALHN 261
Cdd:pfam13492  70 ----LGSAGEDGLPDGPALVVPLVA-GRRVIGVL-ALASSKPRAFDAEDLRLLESLAAQIATAIEN 129
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
364-530 1.09e-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: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   364 YHNWKHAFNVGQFVYgalmssEMGTYFSDLEKAGILIAALSHDLDHRGTNNTFEKKystplgdlysTSTLEHHHFDRAVT 443
Cdd:smart00471   3 YHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAEI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300   444 ILSTEGQNILAalpskqyeqaikqiesAILATDLGRHFSIRKEYkalvddktfdkakREHLDILRSIIMTAGDLSAVTKP 523
Cdd:smart00471  67 LLEEEEPRILE----------------EILRTAILSHHERPDGL-------------RGEPITLEARIVKVADRLDALRA 117

                   ....*..
gi 514696300   524 FPAQRRV 530
Cdd:smart00471 118 DRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
364-539 1.42e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.88  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 364 YHNWKHAFNVGQFVygALMSSEMGTYFSDLEKagILIAALSHDLDHRGTNNTFekkystplgdLYSTSTLEHHHFDRAVT 443
Cdd:cd00077    1 EHRFEHSLRVAQLA--RRLAEELGLSEEDIEL--LRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300 444 ILStegqnilaalpSKQYEQAIKQIESAILATDLgRHFSIRKEYKALVDDKtfdkakrEHLDILRSIIMTAGDLSAVTK- 522
Cdd:cd00077   67 ILR-----------ELLLEEVIKLIDELILAVDA-SHHERLDGLGYPDGLK-------GEEITLEARIVKLADRLDALRr 127
                        170
                 ....*....|....*...
gi 514696300 523 -PFPAQRRVAELVYSEFF 539
Cdd:cd00077  128 dSREKRRRIAEEDLEELL 145
DUF3369 pfam11849
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain ...
102-268 3.38e-04

Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 170 amino acids in length. The domain appears to be related to the GAF domain.


Pssm-ID: 432127 [Multi-domain]  Cd Length: 168  Bit Score: 41.75  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  102 MLDISAALMETTDTKEVVETILQHAAELVHCDRCSLFLYDKETnelssqafdvseegcvgDSDDNQFSFPATTGIagHVA 181
Cdd:pfam11849  24 IIEASADLFELRSLQEFAEGVLTQLAALLNLKKDGLVCVSSGI-----------------AAASGNFYVLAATGK--FES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514696300  182 TTGETLN-IHDAYADDRFNRAIDDKTGFKTRNIlCTPIFDNNDEVIAVTQLinkHGDGPFTERDVKSLNVFAGYCGLALH 260
Cdd:pfam11849  85 LIGKPLSdLLDPEVRELLERALASKRSIFEDDY-VGLYFRTSSGSEGVIYL---ETTRPLSELDRELLEVFCNNISVAFD 160

                  ....*...
gi 514696300  261 NAQLHDQV 268
Cdd:pfam11849 161 NVYLNEEL 168
 
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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