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Conserved domains on  [gi|344925852|ref|NP_001230713|]
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cGMP-dependent 3',5'-cyclic phosphodiesterase isoform PDE2A1 [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;
634-867 2.36e-102

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 2.36e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  634 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 713
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  714 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 789
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344925852  790 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 867
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
388-537 3.93e-30

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: 116.33  E-value: 3.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   388 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 464
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344925852   465 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 537
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
220-366 7.50e-18

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: 81.27  E-value: 7.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   220 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344925852   297 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 366
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
634-867 2.36e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 2.36e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  634 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 713
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  714 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 789
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344925852  790 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 867
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
388-537 3.93e-30

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: 116.33  E-value: 3.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   388 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 464
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344925852   465 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 537
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
634-810 3.16e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.08  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 634 YHNWMHAFSVSHFCYLLYKNLELTnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 713
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 714 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTK 793
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 344925852 794 --GWKTTRKIAELIYKEFF 810
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
305-548 3.38e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.87  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 305 ELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFT 384
Cdd:COG2203  124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALR 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 385 HLDDVSVLLQEIITEARNLSNAEICSVFLLDQN--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 462
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAILLVDEDggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDAST 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 463 HPLFYRGVDDSTG-FRTRNILCFPIKNENqEVIGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 541
Cdd:COG2203  281 DPRFAPSLRELLLaLGIRSLLCVPLLVDG-RLIGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALA 358

                 ....*..
gi 344925852 542 RSHLANE 548
Cdd:COG2203  359 ALLQELA 365
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
220-366 7.50e-18

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: 81.27  E-value: 7.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   220 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344925852   297 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 366
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
388-527 2.86e-16

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: 76.36  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  388 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 467
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  468 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 527
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
633-795 1.46e-14

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: 71.17  E-value: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   633 PYHNWMHAFSVSHFCYLLYKNLELTNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 712
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   713 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnkqHHRLLLCLLMTSCDLSDQT 792
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 344925852   793 KGW 795
Cdd:smart00471 116 RAD 118
GAF COG2203
GAF domain [Signal transduction mechanisms];
24-500 5.24e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.21  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  24 DRLEDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGF 103
Cdd:COG2203   10 AREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 104 SDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPR 183
Cdd:COG2203   90 VATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 184 AVQNPPEGTAEDQKGGAAYTDRDRKILQLCGEL-YDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKV 262
Cdd:COG2203  170 LAGLILDIARLLTQRARLELERLALLNEISQALrSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 263 LGEEVSFPL-TGCLGQVVEDKKSIQLKDLTSEDV---QQLQSMLGCELQAMLCVPVISRatDQVVALACAFNKLEGDlFT 338
Cdd:COG2203  250 EEELGRLPLgEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FT 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 339 DEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNE 418
Cdd:COG2203  327 EEDLELLEALADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELL 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 419 LVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAE 498
Cdd:COG2203  404 LLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALAL 483

                 ..
gi 344925852 499 LV 500
Cdd:COG2203  484 LA 485
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
227-346 6.53e-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: 49.40  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  227 KVLQYLQQETRASRCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSED--VQQLQSMLGC 304
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRNF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 344925852  305 ELQAMLCVPVISRatDQVVALACAFNKleGDLFTDEDEHVIQ 346
Cdd:pfam01590  86 GIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
634-867 2.36e-102

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 318.34  E-value: 2.36e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  634 YHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEgSVMERHHFAQA 713
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDS-SVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  714 IAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVG----YDRNNKQHHRLLLCLLMTSCDLS 789
Cdd:pfam00233  80 FQILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKktldFLENEEDRRLLLLSMLIKAADIS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344925852  790 DQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAY-IPELQISFMEHIAMPIYKLLQDLFPKAAELYERV 867
Cdd:pfam00233 160 NPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTsLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
388-537 3.93e-30

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: 116.33  E-value: 3.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   388 DVSVLLQEIITEARNLSNAEICSVFLLDQN---ELVAKVFDGGvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHP 464
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGL--TLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADP 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344925852   465 LFYRGVDDSTGFrTRNILCFPIKNENQeVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVN 537
Cdd:smart00065  79 LFAEDLLGRYQG-VRSFLAVPLVADGE-LVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
634-810 3.16e-19

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 85.08  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 634 YHNWMHAFSVSHFCYLLYKNLELTnyleDIEIFALFISCMCHDLDHRGTNNSFqvasksvlaalySSEGSVMERHHFAQA 713
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLS----EEDIELLRLAALLHDIGKPGTPDAI------------TEEESELEKDHAIVG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 714 IAILNthgcnifdhfsRKDYQRMLDLMRDIILATDLAHHlrifkdlQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTK 793
Cdd:cd00077   65 AEILR-----------ELLLEEVIKLIDELILAVDASHH-------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                        170
                 ....*....|....*....
gi 344925852 794 --GWKTTRKIAELIYKEFF 810
Cdd:cd00077  127 rdSREKRRRIAEEDLEELL 145
GAF COG2203
GAF domain [Signal transduction mechanisms];
305-548 3.38e-18

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 89.87  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 305 ELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFT 384
Cdd:COG2203  124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALR 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 385 HLDDVSVLLQEIITEARNLSNAEICSVFLLDQN--ELVAKVFDGgvvDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 462
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAILLVDEDggELELVAAPG---LPEEELGRLPLGEGLAGRALRTGEPVVVNDAST 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 463 HPLFYRGVDDSTG-FRTRNILCFPIKNENqEVIGVAELVNKINGPWfSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 541
Cdd:COG2203  281 DPRFAPSLRELLLaLGIRSLLCVPLLVDG-RLIGVLALYSKEPRAF-TEEDLELLEALADQAAIAIERARLYEALEAALA 358

                 ....*..
gi 344925852 542 RSHLANE 548
Cdd:COG2203  359 ALLQELA 365
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
220-366 7.50e-18

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: 81.27  E-value: 7.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   220 DASSLQLKVLQYLQQETRASRCCLLLVSEDNL-QLSCKVI-GDKVLGEEVSFPLT-GCLGQVVEDKKSIQLKDLTSEDVQ 296
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAAdGLTLPTLGIRFPLDeGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344925852   297 QLQSMLGCEL-QAMLCVPVISRatDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQ 366
Cdd:smart00065  81 AEDLLGRYQGvRSFLAVPLVAD--GELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
387-548 4.97e-17

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 79.94  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 387 DDVSVLLQEIITEARNLSNAEICSVFLLDQN----ELVAKVfdgGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYA 462
Cdd:COG3605   17 LDLDEALDRIVRRIAEALGVDVCSIYLLDPDggrlELRATE---GLNPEAVGKVRLPLGEGLVGLVAERGEPLNLADAAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 463 HPLF-YRGVDDSTGFRTrnILCFPIKNENQeVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQY 541
Cdd:COG3605   94 HPRFkYFPETGEEGFRS--FLGVPIIRRGR-VLGVLVVQSREPRE-FTEEEVEFLVTLAAQLAEAIANAELLGELRAALA 169

                 ....*..
gi 344925852 542 RSHLANE 548
Cdd:COG3605  170 ELSLARE 176
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
388-527 2.86e-16

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: 76.36  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  388 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVakVFDGGVVDDESYEIRIPADQGIagHVATTGQILNIPDAYAHPLFY 467
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLE--YLPPGARWLKAAGLEIPPGTGV--TVLRTGRPLVVPDAAGDPRFL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  468 RGVDDSTGFRTRNILCFPIKNENqEVIGVAELVNKinGPWFSKFDEDLATAFSIYCGISI 527
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP--RPPFTEEELELLEVLADQVAIAL 133
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
633-795 1.46e-14

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: 71.17  E-value: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   633 PYHNWMHAFSVSHFCYLLYKNLELTNyledieIFALFISCMCHDLDHRGTNNSFQVASksvlaalyssegSVMERHHFAQ 712
Cdd:smart00471   2 DYHVFEHSLRVAQLAAALAEELGLLD------IELLLLAALLHDIGKPGTPDSFLVKT------------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852   713 AIAILNTHGCNIFDHfsrkdyqrmldlmrdiILATDLAHHLRIFKDLQKmaevgydrnnkqHHRLLLCLLMTSCDLSDQT 792
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSHHERPDGLRG------------EPITLEARIVKVADRLDAL 115

                   ...
gi 344925852   793 KGW 795
Cdd:smart00471 116 RAD 118
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
388-528 2.43e-09

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: 56.32  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  388 DVSVLLQEIITEARNLSNAEICSVFLLDQNELVAkvFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFY 467
Cdd:pfam13185   3 DLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344925852  468 RGVDDSTGFRTrnILCFPIKNENqEVIGVAELVNKINGPwFSKFDEDLATAFSIYCGISIA 528
Cdd:pfam13185  81 GLPAGHAGLRS--FLSVPLVSGG-RVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
GAF COG2203
GAF domain [Signal transduction mechanisms];
24-500 5.24e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.21  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  24 DRLEDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGF 103
Cdd:COG2203   10 AREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 104 SDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPR 183
Cdd:COG2203   90 VATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 184 AVQNPPEGTAEDQKGGAAYTDRDRKILQLCGEL-YDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKV 262
Cdd:COG2203  170 LAGLILDIARLLTQRARLELERLALLNEISQALrSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 263 LGEEVSFPL-TGCLGQVVEDKKSIQLKDLTSEDV---QQLQSMLGCELQAMLCVPVISRatDQVVALACAFNKLEGDlFT 338
Cdd:COG2203  250 EEELGRLPLgEGLAGRALRTGEPVVVNDASTDPRfapSLRELLLALGIRSLLCVPLLVD--GRLIGVLALYSKEPRA-FT 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 339 DEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKcecQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNE 418
Cdd:COG2203  327 EEDLELLEALADQAAIAIERARLYEALEAAL---AALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELL 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 419 LVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAE 498
Cdd:COG2203  404 LLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALAL 483

                 ..
gi 344925852 499 LV 500
Cdd:COG2203  484 LA 485
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
227-346 6.53e-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: 49.40  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  227 KVLQYLQQETRASRCCLLLVSEDNLQLSCkvIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSED--VQQLQSMLGC 304
Cdd:pfam01590   8 TILEELRELLGADRCALYLPDADGLEYLP--PGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPrfLDPLLLLRNF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 344925852  305 ELQAMLCVPVISRatDQVVALACAFNKleGDLFTDEDEHVIQ 346
Cdd:pfam01590  86 GIRSLLAVPIIDD--GELLGVLVLHHP--RPPFTEEELELLE 123
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
368-514 2.69e-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: 45.20  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852 368 LKCECQALLQVAKNLFTHLDDVSVLLQEiitearNLSNAEICSVFLLD-QNELVAKVFDGGVVddesyEIRIPADQGIAG 446
Cdd:COG1956   12 LLAQLSALLAGETDLIANLANISALLFE------ALPDYNWVGFYLVDgGGELVLGPFQGPPA-----CTRIPFGKGVCG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344925852 447 HVATTGQILNIPDAYAHPLFYRgvDDSTgfrTRNILCFPIKNeNQEVIGVAElvnkINGPWFSKFDED 514
Cdd:COG1956   81 TAAAEGETQLVPDVHAFPGHIA--CDSA---SRSEIVVPIFK-DGEVIGVLD----IDSPTPGRFDEE 138
GAF_3 pfam13492
GAF domain;
388-529 7.49e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 43.51  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  388 DVSVLLQEIITEARNLSNAEICSVFLLD--QNEL-VAKVFDGGVVDDESyeirIPADQGIAGHVATTGQilnipdayahP 464
Cdd:pfam13492   1 SLDEILEALLKLLVRLLGAERAAVYLLDedGNKLqVAAGYDGEPDPSES----LDADSPLARRALSSGE----------P 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344925852  465 LFYRGVDDSTGFRTRNILCFPIKNENQeVIGVaeLVnkINGPWFSKFDED---LATAFSIYCGISIAH 529
Cdd:pfam13492  67 ISGLGSAGEDGLPDGPALVVPLVAGRR-VIGV--LA--LASSKPRAFDAEdlrLLESLAAQIATAIEN 129
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
228-346 1.09e-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: 43.22  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344925852  228 VLQYLQQETRASRCCLLLVSEDNlQLSCKVIGDKVLGEEVSFPL-TGCLGQVVEDKKSIQLKDLTSEDVQQLQSMLGCEL 306
Cdd:pfam13185  11 VLEAAVELGASAVGFILLVDDDG-RLAAWGGAADELSAALDDPPgEGLVGEALRTGRPVIVNDLAADPAKKGLPAGHAGL 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 344925852  307 QAMLCVPVISRatDQVVALACAFNKLEGDlFTDEDEHVIQ 346
Cdd:pfam13185  90 RSFLSVPLVSG--GRVVGVLALGSNRPGA-FDEEDLELLE 126
 
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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