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Conserved domains on  [gi|326205401|dbj|BAJ84077|]
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rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
477-721 2.01e-105

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 2.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  477 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 555
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  556 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 635
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  636 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 715
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 326205401  716 PMLDGI 721
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
173-360 1.16e-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: 1.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   173 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 252
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   253 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 332
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 326205401   333 EMDETLMESLTQFLGWSVLNPDTYESMN 360
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
477-721 2.01e-105

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 2.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  477 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 555
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  556 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 635
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  636 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 715
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 326205401  716 PMLDGI 721
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
173-360 1.16e-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: 1.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   173 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 252
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   253 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 332
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 326205401   333 EMDETLMESLTQFLGWSVLNPDTYESMN 360
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
476-576 7.43e-09

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 54.61  E-value: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   476 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 555
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 326205401   556 TLLRDESLNIFQNLNR---RQHEH 576
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
173-350 2.37e-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: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  173 DIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtpdgreinfYKVIDYILHGKEDIKVIP 252
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD----------------------------------ADGLEYLPPGARWLKAAG 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  253 NPPPDhwalvsGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFD 332
Cdd:pfam01590  47 LEIPP------GTGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFT 115
                         170
                  ....*....|....*...
gi 326205401  333 EMDETLMESLTQFLGWSV 350
Cdd:pfam01590 116 EEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
477-662 3.17e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.42  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 477 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 556
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 557 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 636
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 326205401 637 ACDLSAITK--PWEVQSQVALLVAAEFW 662
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
172-365 3.09e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.96  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 172 TDIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtPDGREINFYKVIDyilhgkedikvI 251
Cdd:COG2203  206 LDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGELELVAAPG-----------L 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 252 PNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFA-FQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkP 330
Cdd:COG2203  249 PEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-A 324
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 326205401 331 FDEMDETLMESLTQFLGWSVLNPDTYESMNKLENR 365
Cdd:COG2203  325 FTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
477-721 2.01e-105

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 2.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  477 YHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHG-SSILERHHLEFGK 555
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNdSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  556 TLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYeseqewtQYMMLEQTRKEIVMAMMM 635
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTL-------DFLENEEDRRLLLLSMLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  636 TACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTvLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEIT 715
Cdd:pfam00233 154 KAADISNPTRPWEISKKWADLVAEEFFRQGDLEKE-LGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQ 232

                  ....*.
gi 326205401  716 PMLDGI 721
Cdd:pfam00233 233 PLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
173-360 1.16e-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: 1.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   173 DIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEffdVWPVLMGEVPPYsgprtpdgreinfykvidyilhgkedikvip 252
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGE---LVLVAADGLTLP------------------------------- 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   253 nPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAfqkEPLDESGWMIKNVLSMPIVNKkEEIVGVATFYNRKDGKPFD 332
Cdd:smart00065  47 -TLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA---EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSPRPFT 121
                          170       180
                   ....*....|....*....|....*...
gi 326205401   333 EMDETLMESLTQFLGWSVLNPDTYESMN 360
Cdd:smart00065 122 EEDEELLQALANQLAIALANAQLYEELR 149
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
476-576 7.43e-09

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 54.61  E-value: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401   476 TYHNWRHGFNVGQTMFsllvtgKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKsqnplaklhgSSILERHHLEFGK 555
Cdd:smart00471   2 DYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK----------TSVLEDHHFIGAE 65
                           90       100
                   ....*....|....*....|....
gi 326205401   556 TLLRDESLNIFQNLNR---RQHEH 576
Cdd:smart00471  66 ILLEEEEPRILEEILRtaiLSHHE 89
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
173-350 2.37e-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: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  173 DIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtpdgreinfYKVIDYILHGKEDIKVIP 252
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPD----------------------------------ADGLEYLPPGARWLKAAG 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401  253 NPPPDhwalvsGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGwmIKNVLSMPIVNkKEEIVGVATFYNRKDgkPFD 332
Cdd:pfam01590  47 LEIPP------GTGVTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFG--IRSLLAVPIID-DGELLGVLVLHHPRP--PFT 115
                         170
                  ....*....|....*...
gi 326205401  333 EMDETLMESLTQFLGWSV 350
Cdd:pfam01590 116 EEELELLEVLADQVAIAL 133
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
477-662 3.17e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 50.42  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 477 YHNWRHGFNVGQTMFSLLvtgkLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYqmksqnplakLHGSSILERHHLEFGKT 556
Cdd:cd00077    1 EHRFEHSLRVAQLARRLA----EELGLSEEDIELLRLAALLHDIGKPGTPDAI----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 557 LLRDESLnifqnlnrrqhEHAIHMMDIAIIATDLALYFKKRTMfqkivdqsktyeseqewtQYMMLEQTRKEIVMAMMMT 636
Cdd:cd00077   67 ILRELLL-----------EEVIKLIDELILAVDASHHERLDGL------------------GYPDGLKGEEITLEARIVK 117
                        170       180
                 ....*....|....*....|....*...
gi 326205401 637 ACDLSAITK--PWEVQSQVALLVAAEFW 662
Cdd:cd00077  118 LADRLDALRrdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
172-365 3.09e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.96  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 172 TDIERQFHKALYTVRAFLNCDRYSVGLLDmtkqkeffdvwpvlmgevppysgprtPDGREINFYKVIDyilhgkedikvI 251
Cdd:COG2203  206 LDLEELLQRILELAGELLGADRGAILLVD--------------------------EDGGELELVAAPG-----------L 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326205401 252 PNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFA-FQKEPLDESGwmIKNVLSMPIVNKkEEIVGVATFYNRKDGkP 330
Cdd:COG2203  249 PEEELGRLPLGEGLAGRALRTGEPVVVNDASTDPRFApSLRELLLALG--IRSLLCVPLLVD-GRLIGVLALYSKEPR-A 324
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 326205401 331 FDEMDETLMESLTQFLGWSVLNPDTYESMNKLENR 365
Cdd:COG2203  325 FTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
 
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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