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Conserved domains on  [gi|530377607|ref|XP_005263013|]
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guanylate cyclase soluble subunit alpha-1 isoform X3 [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;
237-408 2.79e-91

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 274.51  E-value: 2.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  237 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 316
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  317 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 396
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 530377607  397 FVFTPRSREELP 408
Cdd:pfam00211 160 FEFTERGEIEVK 171
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
42-231 5.16e-60

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: 195.10  E-value: 5.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   42 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 117
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  118 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 179
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530377607  180 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 231
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
237-408 2.79e-91

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 274.51  E-value: 2.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  237 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 316
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  317 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 396
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 530377607  397 FVFTPRSREELP 408
Cdd:pfam00211 160 FEFTERGEIEVK 171
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
210-399 4.21e-89

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: 269.51  E-value: 4.21e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   210 EEKKKTVDLLCSIFPCEVAQQLWQG-QVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVY 288
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   289 KVETIGDAYCVAGGLHKE-SDTHAVQIALMALKMMELSDEVMSPH-GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNV 366
Cdd:smart00044  81 KVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVQHrEEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTV 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 530377607   367 TLANKFESCSVPRKINVSPTTYRLL-KDCPGFVF 399
Cdd:smart00044 161 NLASRMESAGDPGQIQVSEETYSLLaRRGGQFVF 194
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
42-231 5.16e-60

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: 195.10  E-value: 5.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   42 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 117
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  118 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 179
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530377607  180 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 231
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
244-407 1.09e-59

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: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 244 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMME 323
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 324 LSDEVMSPH--GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcPGFVFTP 401
Cdd:cd07302   81 ALAELNAERegGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGD-AGFEFEE 159

                 ....*.
gi 530377607 402 RSREEL 407
Cdd:cd07302  160 LGEVEL 165
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
173-407 5.83e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 142.64  E-value: 5.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 173 ALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQG--QVVQAKKFSNVTMLFS 250
Cdd:COG2114  149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 251 DIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMM----ELSD 326
Cdd:COG2114  229 DIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQealaELNA 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 327 EVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPR-YCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcpGFVFTPRSRE 405
Cdd:COG2114  309 ELPAEGGPPLRVRIGIHTGEVVVGNIGSEDRLdYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD--RFEFRELGEV 386

                 ..
gi 530377607 406 EL 407
Cdd:COG2114  387 RL 388
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
237-408 2.79e-91

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 274.51  E-value: 2.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  237 VQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIAL 316
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  317 MALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKdCPG 396
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLK-TEG 159
                         170
                  ....*....|..
gi 530377607  397 FVFTPRSREELP 408
Cdd:pfam00211 160 FEFTERGEIEVK 171
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
210-399 4.21e-89

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: 269.51  E-value: 4.21e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   210 EEKKKTVDLLCSIFPCEVAQQLWQG-QVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVY 288
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   289 KVETIGDAYCVAGGLHKE-SDTHAVQIALMALKMMELSDEVMSPH-GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNV 366
Cdd:smart00044  81 KVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVQHrEEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTV 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 530377607   367 TLANKFESCSVPRKINVSPTTYRLL-KDCPGFVF 399
Cdd:smart00044 161 NLASRMESAGDPGQIQVSEETYSLLaRRGGQFVF 194
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
42-231 5.16e-60

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: 195.10  E-value: 5.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607   42 IPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPnFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRR---- 117
Cdd:pfam07701   3 ISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKK-LTDVFRLRRPLIEFTFDNILQHINVVFELQTKRpllr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607  118 ------------------WDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVL 179
Cdd:pfam07701  82 keeeaklsaaldaseeesSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530377607  180 IGEQARAQDGLKK-RLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQL 231
Cdd:pfam07701 162 AGQQQSAELKLALdQLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
244-407 1.09e-59

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: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 244 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMME 323
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 324 LSDEVMSPH--GEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcPGFVFTP 401
Cdd:cd07302   81 ALAELNAERegGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGD-AGFEFEE 159

                 ....*.
gi 530377607 402 RSREEL 407
Cdd:cd07302  160 LGEVEL 165
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
173-407 5.83e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 142.64  E-value: 5.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 173 ALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQG--QVVQAKKFSNVTMLFS 250
Cdd:COG2114  149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 251 DIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMM----ELSD 326
Cdd:COG2114  229 DIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQealaELNA 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 327 EVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPR-YCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDcpGFVFTPRSRE 405
Cdd:COG2114  309 ELPAEGGPPLRVRIGIHTGEVVVGNIGSEDRLdYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD--RFEFRELGEV 386

                 ..
gi 530377607 406 EL 407
Cdd:COG2114  387 RL 388
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
244-381 8.62e-30

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: 8.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377607 244 NVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLhkesdTHAVQIALMALKMME 323
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-----DHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377607 324 LSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKmPRYCLFGNNVTLANKFESCSVPRKI 381
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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