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Conserved domains on  [gi|1958657211|ref|XP_038941414|]
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calmodulin-binding transcription activator 2 isoform X4 [Rattus norvegicus]

Protein Classification

calmodulin-binding transcription activator( domain architecture ID 12224848)

calmodulin-binding transcription activator may act as a tumor suppressor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
57-173 2.75e-70

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


:

Pssm-ID: 198144  Cd Length: 118  Bit Score: 230.37  E-value: 2.75e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657211   136 ECLYGCYVHSSIVPTFHRRCYWLLQNPDIVLVHYLNVP 173
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
558-638 6.11e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


:

Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 57.07  E-value: 6.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  558 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 635
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81

                   ...
gi 1958657211  636 FEY 638
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-835 1.26e-09

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  734 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 812
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217
                           90       100
                   ....*....|....*....|...
gi 1958657211  813 LGRLPLSVAHSRGHVRLARCLEE 835
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
767-906 1.94e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  767 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 846
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657211  847 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 906
Cdd:PTZ00322   179 -----ANAKPDS--------FTGKPPSLEDSPISSHHPDFSAVPQPMMGSLIViMVGLPGR 226
 
Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
57-173 2.75e-70

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 198144  Cd Length: 118  Bit Score: 230.37  E-value: 2.75e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657211   136 ECLYGCYVHSSIVPTFHRRCYWLLQNPDIVLVHYLNVP 173
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
63-172 2.44e-54

CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues containing a predicted bipartite NLS and named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 461077  Cd Length: 114  Bit Score: 184.78  E-value: 2.44e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211   63 RWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGMECLYGC 141
Cdd:pfam03859    3 RWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIHCY 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958657211  142 YVHSSIVPTFHRRCYWLLQNP-DIVLVHYLNV 172
Cdd:pfam03859   83 YAHSEDNPTFQRRIYWLLDSDyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
558-638 6.11e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 57.07  E-value: 6.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  558 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 635
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81

                   ...
gi 1958657211  636 FEY 638
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-835 1.26e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  734 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 812
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217
                           90       100
                   ....*....|....*....|...
gi 1958657211  813 LGRLPLSVAHSRGHVRLARCLEE 835
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
739-831 1.12e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  739 LHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLfcWNRQALSIPDSlGRLPL 818
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDN-GRTAL 65
                           90
                   ....*....|...
gi 1958657211  819 SVAHSRGHVRLAR 831
Cdd:pfam12796   66 HYAARSGHLEIVK 78
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
767-906 1.94e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  767 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 846
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657211  847 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 906
Cdd:PTZ00322   179 -----ANAKPDS--------FTGKPPSLEDSPISSHHPDFSAVPQPMMGSLIViMVGLPGR 226
 
Name Accession Description Interval E-value
CG-1 smart01076
CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains ...
57-173 2.75e-70

CG-1 domains are highly conserved domains of about 130 amino-acid residues; The domains contain a predicted bipartite NLS and are named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 198144  Cd Length: 118  Bit Score: 230.37  E-value: 2.75e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657211   136 ECLYGCYVHSSIVPTFHRRCYWLLQNPDIVLVHYLNVP 173
Cdd:smart01076   81 ECLHCYYAHSEINPTFHRRCYWLLQNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
63-172 2.44e-54

CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues containing a predicted bipartite NLS and named after a partial cDNA clone isolated from parsley encoding a sequence-specific DNA-binding protein. CG-1 domains are associated with CAMTA proteins (for CAlModulin -binding Transcription Activator) that are transcription factors containing a calmodulin -binding domain and ankyrins (ANK) motifs.


Pssm-ID: 461077  Cd Length: 114  Bit Score: 184.78  E-value: 2.44e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211   63 RWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGMECLYGC 141
Cdd:pfam03859    3 RWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEAIHCY 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958657211  142 YVHSSIVPTFHRRCYWLLQNP-DIVLVHYLNV 172
Cdd:pfam03859   83 YAHSEDNPTFQRRIYWLLDSDyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
558-638 6.11e-10

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 57.07  E-value: 6.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  558 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 635
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81

                   ...
gi 1958657211  636 FEY 638
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-835 1.26e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  734 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 812
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217
                           90       100
                   ....*....|....*....|...
gi 1958657211  813 LGRLPLSVAHSRGHVRLARCLEE 835
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-835 3.41e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 3.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  734 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 812
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLL------------LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL--EAGAdVNARDN 184
                           90       100
                   ....*....|....*....|...
gi 1958657211  813 LGRLPLSVAHSRGHVRLARCLEE 835
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
735-833 3.14e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 3.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  735 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDSL 813
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLL------------LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL--EAGAdVNAQDND 152
                           90       100
                   ....*....|....*....|
gi 1958657211  814 GRLPLSVAHSRGHVRLARCL 833
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
739-831 1.12e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  739 LHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLfcWNRQALSIPDSlGRLPL 818
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDN-GRTAL 65
                           90
                   ....*....|...
gi 1958657211  819 SVAHSRGHVRLAR 831
Cdd:pfam12796   66 HYAARSGHLEIVK 78
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
767-906 1.94e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657211  767 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 846
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657211  847 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 906
Cdd:PTZ00322   179 -----ANAKPDS--------FTGKPPSLEDSPISSHHPDFSAVPQPMMGSLIViMVGLPGR 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
735-801 1.64e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 1.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958657211  735 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEAdpLNVDHFSCTPLMWACALGHLEAAVLLFC 801
Cdd:pfam12796   30 GRTALHLAAKNGHLEIVKLL------------LEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLE 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
769-821 4.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 4.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958657211  769 QEADPLNVDH---FSCTPLMWACALGHLEAAVLLFCwNRQALSIPDSLGRLPLSVA 821
Cdd:pfam13857    2 LEHGPIDLNRldgEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
735-799 5.75e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958657211  735 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLL 799
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLL------------LEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
 
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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