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Conserved domains on  [gi|1958657214|ref|XP_038941415|]
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calmodulin-binding transcription activator 2 isoform X6 [Rattus norvegicus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11648726)

ankyrin repeat (ANK) domain-containing protein mediates specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CG-1 super family cl04295
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 57-149 3.37e-46

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.


The actual alignment was detected with superfamily member smart01076:

Pssm-ID: 470995  Cd Length: 118  Bit Score: 161.42  E-value: 3.37e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657214   136 E------------------------NPDIVLVHYLNVP 149
Cdd:smart01076   81 EclhcyyahseinptfhrrcywllqNPDIVLVHYLNVP 118
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 534-614 6.02e-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: 6.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  534 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 611
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81


                   ...
gi 1958657214  612 FEY 614
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-811 1.23e-09

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  710 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 788
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217

                           90       100
                   ....*....|....*....|...
gi 1958657214  789 LGRLPLSVAHSRGHVRLARCLEE 811
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 743-882 1.88e-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: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  743 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 822
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657214  823 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 882
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 ...
 57-149 3.37e-46

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: 161.42  E-value: 3.37e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657214   136 E------------------------NPDIVLVHYLNVP 149
Cdd:smart01076   81 EclhcyyahseinptfhrrcywllqNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 63-148 2.09e-33

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: 124.69  E-value: 2.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214   63 RWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGME----- 136
Cdd:pfam03859    3 RWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEaihcy 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958657214  137 ------NP--------------DIVLVHYLNV 148
Cdd:pfam03859   83 yahsedNPtfqrriywlldsdyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 534-614 6.02e-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: 6.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  534 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 611
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81


                   ...
gi 1958657214  612 FEY 614
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-811 1.23e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  710 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 788
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217

                           90       100
                   ....*....|....*....|...
gi 1958657214  789 LGRLPLSVAHSRGHVRLARCLEE 811
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
715-807 1.10e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  715 LHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLfcWNRQALSIPDSlGRLPL 794
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDN-GRTAL 65

                           90
                   ....*....|...
gi 1958657214  795 SVAHSRGHVRLAR 807
Cdd:pfam12796   66 HYAARSGHLEIVK 78
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 743-882 1.88e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  743 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 822
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657214  823 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 882
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 ...
 57-149 3.37e-46

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: 161.42  E-value: 3.37e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214    57 LPPERLRWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGM 135
Cdd:smart01076    1 LPEAKHRWLTPEEIAAILINFDKHTEWLTTSPPTRPKSGSLFLFNRKKLKYfRKDGYNWKKKKDGKTVREDHEKLKVGGI 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1958657214   136 E------------------------NPDIVLVHYLNVP 149
Cdd:smart01076   81 EclhcyyahseinptfhrrcywllqNPDIVLVHYLNVP 118
CG-1 pfam03859
CG-1 domain; CG-1 domains are highly conserved domains of about 130 amino-acid residues ...
 63-148 2.09e-33

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: 124.69  E-value: 2.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214   63 RWNTNEEIASYLITFEKHDEWLSCAPKTRPQNGSIILYNRKKVKY-RKDGYLWKKRKDGKTTREDHMKLKVQGME----- 136
Cdd:pfam03859    3 RWLKPQEILAILLNYDPYGFCITPEPPPRPPSGSLFLFDRKKLRYfRKDGHNWRKKKDGKTVREDHEKLKVGGVEaihcy 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958657214  137 ------NP--------------DIVLVHYLNV 148
Cdd:pfam03859   83 yahsedNPtfqrriywlldsdyHIVLVHYLNV 114
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 534-614 6.02e-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: 6.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  534 TITDFSPEWSYPEGGVKVLITGP-WTEAAEHYSCVFDHIAVPASLVQPGVLRCYCPAHEVGLVSLQVAGREGPL-SASVL 611
Cdd:pfam01833    2 VITSISPSSGPASGGTTITITGSnFGTDSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIsSSPLT 81


                   ...
gi 1958657214  612 FEY 614
Cdd:pfam01833   82 FTY 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-811 1.23e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  710 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 788
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLL------------LEAGADVNARDNDGETPLHLAAENGHLEIVKLLL--EAGAdVNAKDN 217

                           90       100
                   ....*....|....*....|...
gi 1958657214  789 LGRLPLSVAHSRGHVRLARCLEE 811
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-811 3.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 3.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  710 RGMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDS 788
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLL------------LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL--EAGAdVNARDN 184

                           90       100
                   ....*....|....*....|...
gi 1958657214  789 LGRLPLSVAHSRGHVRLARCLEE 811
Cdd:COG0666    185 DGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
711-809 3.09e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 3.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  711 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFcwNRQA-LSIPDSL 789
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLL------------LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL--EAGAdVNAQDND 152

                           90       100
                   ....*....|....*....|
gi 1958657214  790 GRLPLSVAHSRGHVRLARCL 809
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
715-807 1.10e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  715 LHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLLfcWNRQALSIPDSlGRLPL 794
Cdd:pfam12796    1 LHLAAKNGNLELVKLL------------LENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDN-GRTAL 65

                           90
                   ....*....|...
gi 1958657214  795 SVAHSRGHVRLAR 807
Cdd:pfam12796   66 HYAARSGHLEIVK 78
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 743-882 1.88e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657214  743 LEQEADPLNVDHFSCTPLMWACALGHLEAAVLLFCWNRQAlSIPDSLGRLPLSVAHSRGHVRLARCLEELQRQELSVEhp 822
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG-- 178

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958657214  823 lalspQSSSPDTglssvsspSELSDGTFSVTSAYSSAPDGSPPPAPMLASEIS-METIPGQ 882
Cdd:PTZ00322   179 -----ANAKPDS--------FTGKPPSLEDSPISSHHPDFSAVPQPMMGSLIViMVGLPGR 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
711-777 1.61e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 1.61e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958657214  711 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEAdpLNVDHFSCTPLMWACALGHLEAAVLLFC 777
Cdd:pfam12796   30 GRTALHLAAKNGHLEIVKLL------------LEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLE 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
745-797 3.98e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958657214  745 QEADPLNVDH---FSCTPLMWACALGHLEAAVLLFCwNRQALSIPDSLGRLPLSVA 797
Cdd:pfam13857    2 LEHGPIDLNRldgEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
711-775 5.67e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.67e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958657214  711 GMSLLHLAAAQGYARLIETLsqwrsvetgsldLEQEADPLNVDHFSCTPLMWACALGHLEAAVLL 775
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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