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Conserved domains on  [gi|1694538755|ref|XP_029475547|]
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potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1-like [Rhinatrema bivittatum]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10034975)

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP) where binding of the effector leads to conformational changes; may be involved in regulating transcription, be present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK), or be part of vertebrate cyclic nucleotide-gated ion-channels.

CATH:  2.60.120.10
Gene Ontology:  GO:0030552|GO:0030551
PubMed:  6280140|12087135|17601606|11734894
SCOP:  4000272

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 84-192 6.65e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 110.11  E-value: 6.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  84 LFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMK---LTDGSYFGEICLLTKGRR 158
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgREQIvgfLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1694538755 159 TASVRADTYCRLYSLSVDHFNEVLEEYPMMRRAF 192
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 282-505 2.25e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  282 PAPSPQTPQQSMVLSPCSYTTAvcsPPVQSPLASRTFQYGSPTASQLSLIQQQQQAPASSKKNEAHKSTQALHNTNLTRE 361
Cdd:PRK10263   362 PVPGPQTGEPVIAPAPEGYPQQ---SQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAP 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  362 VRPLSASQ----PSLPHEISTPI-----TRLHPTVGESLASIPQPISSIQGTGIQAGNRSTVPQRVSLF----------- 421
Cdd:PRK10263   439 EQPVAGNAwqaeEQQSTFAPQSTyqteqTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYyfeeveekrar 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  422 -RQMSSGALPPIRGAAPQlppasvsspspsaspvPAPAPTSVSAPAPASVPIPTPVSTSAPALSPNRDSSAVLSTDPEAD 500
Cdd:PRK10263   519 eREQLAAWYQPIPEPVKE----------------PEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVA 582


                   ....*
gi 1694538755  501 KPRYA 505
Cdd:PRK10263   583 APVFS 587
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 84-192 6.65e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 110.11  E-value: 6.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  84 LFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMK---LTDGSYFGEICLLTKGRR 158
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgREQIvgfLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1694538755 159 TASVRADTYCRLYSLSVDHFNEVLEEYPMMRRAF 192
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 84-193 5.95e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 5.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755   84 LFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEM---KLTDGSYFGEICLLTKGRR 158
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgEEQivgTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1694538755  159 TASVRADTY--CRLYSLSVDHFNEVLEEYPMMRRAFE 193
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 85-213 1.09e-18

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 84.27  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  85 FANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMKL---TDGSYFGEICLLTKGRRT 159
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgREQILgflGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1694538755 160 ASVRADTYCRLYSLSVDHFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQR 213
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 102-185 6.42e-18

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.42  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755 102 FEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMK---LTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVD 176
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgREQIlavLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 1694538755 177 HFNEVLEEY 185
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
111-186 1.43e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 51.91  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755 111 IIREGAVGKKMYFIQHGVAGVIAKSS--KEMKLT---DGSYFGEICLLTKG-RRTASVRADTYCRLYSLSVDHFNEVLEE 184
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMILSylnQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110


                  ..
gi 1694538755 185 YP 186
Cdd:PRK11753  111 NP 112
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 282-505 2.25e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  282 PAPSPQTPQQSMVLSPCSYTTAvcsPPVQSPLASRTFQYGSPTASQLSLIQQQQQAPASSKKNEAHKSTQALHNTNLTRE 361
Cdd:PRK10263   362 PVPGPQTGEPVIAPAPEGYPQQ---SQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAP 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  362 VRPLSASQ----PSLPHEISTPI-----TRLHPTVGESLASIPQPISSIQGTGIQAGNRSTVPQRVSLF----------- 421
Cdd:PRK10263   439 EQPVAGNAwqaeEQQSTFAPQSTyqteqTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYyfeeveekrar 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  422 -RQMSSGALPPIRGAAPQlppasvsspspsaspvPAPAPTSVSAPAPASVPIPTPVSTSAPALSPNRDSSAVLSTDPEAD 500
Cdd:PRK10263   519 eREQLAAWYQPIPEPVKE----------------PEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVA 582


                   ....*
gi 1694538755  501 KPRYA 505
Cdd:PRK10263   583 APVFS 587
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 84-192 6.65e-29

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 110.11  E-value: 6.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  84 LFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMK---LTDGSYFGEICLLTKGRR 158
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgREQIvgfLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1694538755 159 TASVRADTYCRLYSLSVDHFNEVLEEYPMMRRAF 192
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 84-193 5.95e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 5.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755   84 LFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEM---KLTDGSYFGEICLLTKGRR 158
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgEEQivgTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1694538755  159 TASVRADTY--CRLYSLSVDHFNEVLEEYPMMRRAFE 193
Cdd:smart00100  81 AASAAAVALelATLLRIDFRDFLQLLPELPQLLLELL 117
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 85-213 1.09e-18

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 84.27  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  85 FANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMKL---TDGSYFGEICLLTKGRRT 159
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgREQILgflGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1694538755 160 ASVRADTYCRLYSLSVDHFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQR 213
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFL 134
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 102-185 6.42e-18

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.42  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755 102 FEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAKSS--KEMK---LTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVD 176
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgREQIlavLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*....
gi 1694538755 177 HFNEVLEEY 185
Cdd:pfam00027  81 DFLELLERD 89
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
111-186 1.43e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 51.91  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755 111 IIREGAVGKKMYFIQHGVAGVIAKSS--KEMKLT---DGSYFGEICLLTKG-RRTASVRADTYCRLYSLSVDHFNEVLEE 184
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegKEMILSylnQGDFIGELGLFEEGqERSAWVRAKTACEVAEISYKKFRQLIQV 110


                  ..
gi 1694538755 185 YP 186
Cdd:PRK11753  111 NP 112
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 100-148 8.21e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 41.63  E-value: 8.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1694538755 100 LRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVIAK----SSKEMKLTDGSYFG 148
Cdd:PLN02868   31 VVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPaeeeSRPEFLLKRYDYFG 83
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 282-505 2.25e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  282 PAPSPQTPQQSMVLSPCSYTTAvcsPPVQSPLASRTFQYGSPTASQLSLIQQQQQAPASSKKNEAHKSTQALHNTNLTRE 361
Cdd:PRK10263   362 PVPGPQTGEPVIAPAPEGYPQQ---SQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAP 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  362 VRPLSASQ----PSLPHEISTPI-----TRLHPTVGESLASIPQPISSIQGTGIQAGNRSTVPQRVSLF----------- 421
Cdd:PRK10263   439 EQPVAGNAwqaeEQQSTFAPQSTyqteqTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYyfeeveekrar 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694538755  422 -RQMSSGALPPIRGAAPQlppasvsspspsaspvPAPAPTSVSAPAPASVPIPTPVSTSAPALSPNRDSSAVLSTDPEAD 500
Cdd:PRK10263   519 eREQLAAWYQPIPEPVKE----------------PEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVA 582


                   ....*
gi 1694538755  501 KPRYA 505
Cdd:PRK10263   583 APVFS 587
 
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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