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Conserved domains on  [gi|1829778962|ref|NP_001366599|]
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guanylate cyclase soluble subunit alpha-1 isoform A [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
472-643 4.16e-89

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 276.05  E-value: 4.16e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 472 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 551
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 552 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 631
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 1829778962 632 FVFTPRSREELP 643
Cdd:pfam00211 160 FEFTERGEIEVK 171
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
277-466 3.21e-58

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


:

Pssm-ID: 462234  Cd Length: 214  Bit Score: 195.87  E-value: 3.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 277 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 352
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 353 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 414
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1829778962 415 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 466
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
472-643 4.16e-89

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 276.05  E-value: 4.16e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 472 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 551
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 552 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 631
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 1829778962 632 FVFTPRSREELP 643
Cdd:pfam00211 160 FEFTERGEIEVK 171
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
445-634 1.12e-86

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 269.90  E-value: 1.12e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962  445 EEKKKTVDLLCSIFPCEVAQQLWQG-QVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVY 523
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962  524 KVETIGDAYCVAGGLHKE-SDTHAVQIALMALKMMELSDEVMSPH-GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNV 601
Cdd:smart00044  81 KVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVQHrEEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTV 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1829778962  602 TLANKFESCSVPRKINVSPTTYRLL-KDCPGFVF 634
Cdd:smart00044 161 NLASRMESAGDPGQIQVSEETYSLLaRRGGQFVF 194
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
277-466 3.21e-58

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


Pssm-ID: 462234  Cd Length: 214  Bit Score: 195.87  E-value: 3.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 277 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 352
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 353 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 414
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1829778962 415 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 466
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
479-642 9.99e-58

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 193.18  E-value: 9.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 479 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMME 558
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 559 LSDEVMSPH--GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcPGFVFTP 636
Cdd:cd07302    81 ALAELNAERegGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGD-AGFEFEE 159

                  ....*.
gi 1829778962 637 RSREEL 642
Cdd:cd07302   160 LGEVEL 165
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
408-642 8.75e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 142.64  E-value: 8.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 408 ALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQG--QVVQAKKFSNVTMLFS 485
Cdd:COG2114   149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 486 DIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMM----ELSD 561
Cdd:COG2114   229 DIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQealaELNA 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 562 EVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPR-YCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcpGFVFTPRSRE 640
Cdd:COG2114   309 ELPAEGGPPLRVRIGIHTGEVVVGNIGSEDRLdYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD--RFEFRELGEV 386

                  ..
gi 1829778962 641 EL 642
Cdd:COG2114   387 RL 388
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
472-643 4.16e-89

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 276.05  E-value: 4.16e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 472 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 551
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 552 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 631
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 1829778962 632 FVFTPRSREELP 643
Cdd:pfam00211 160 FEFTERGEIEVK 171
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
445-634 1.12e-86

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 269.90  E-value: 1.12e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962  445 EEKKKTVDLLCSIFPCEVAQQLWQG-QVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVY 523
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962  524 KVETIGDAYCVAGGLHKE-SDTHAVQIALMALKMMELSDEVMSPH-GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNV 601
Cdd:smart00044  81 KVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVQHrEEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTV 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1829778962  602 TLANKFESCSVPRKINVSPTTYRLL-KDCPGFVF 634
Cdd:smart00044 161 NLASRMESAGDPGQIQVSEETYSLLaRRGGQFVF 194
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
277-466 3.21e-58

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


Pssm-ID: 462234  Cd Length: 214  Bit Score: 195.87  E-value: 3.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 277 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 352
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 353 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 414
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1829778962 415 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 466
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
479-642 9.99e-58

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 193.18  E-value: 9.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 479 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMME 558
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 559 LSDEVMSPH--GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcPGFVFTP 636
Cdd:cd07302    81 ALAELNAERegGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGD-AGFEFEE 159

                  ....*.
gi 1829778962 637 RSREEL 642
Cdd:cd07302   160 LGEVEL 165
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
408-642 8.75e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 142.64  E-value: 8.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 408 ALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQG--QVVQAKKFSNVTMLFS 485
Cdd:COG2114   149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 486 DIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMM----ELSD 561
Cdd:COG2114   229 DIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQealaELNA 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 562 EVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPR-YCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcpGFVFTPRSRE 640
Cdd:COG2114   309 ELPAEGGPPLRVRIGIHTGEVVVGNIGSEDRLdYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD--RFEFRELGEV 386

                  ..
gi 1829778962 641 EL 642
Cdd:COG2114   387 RL 388
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
479-616 3.42e-29

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 112.83  E-value: 3.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829778962 479 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLhkesdTHAVQIALMALKMME 558
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-----DHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1829778962 559 LSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKmPRYCLFGNNVTLANKFESCSVPRKI 616
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQV 132
 
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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