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Conserved domains on  [gi|971377283|ref|XP_015130705|]
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dachshund homolog 1 isoform X3 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 140-234 5.61e-71

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


:

Pssm-ID: 410784  Cd Length: 95  Bit Score: 225.70  E-value: 5.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 140 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 219
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 971377283 220 LISRKDFETLYNDCT 234
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 339-452 3.48e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283  339 EKLQSPPTQG---------SQASINHPNLPGQHNVPvshPLNPLQQNHLLPNGlelpfmmmPHPLIPVSLPPASVTMAMS 409
Cdd:pfam03154 422 QQLPPPPAQPpvltqsqslPPPAASHPPTSGLHQVP---SQSPFPQHPFVPGG--------PPPITPPSGPPTSTSSAMP 490

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 971377283  410 QMNHLSTIANMAAAAQVQSPPSRVETSVIKERVPD-------------SPSPAPSL 452
Cdd:pfam03154 491 GIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDeaeepesppppprSPSPEPTV 546
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 140-234 5.61e-71

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 225.70  E-value: 5.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 140 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 219
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 971377283 220 LISRKDFETLYNDCT 234
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 135-235 4.99e-43

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 150.50  E-value: 4.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283  135 NTPQNNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPG 214
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPS 79

                          90       100
                  ....*....|....*....|.
gi 971377283  215 VNRCKLISRKDFETLYNDCTN 235
Cdd:pfam02437  80 VRRCGLITKTDAERLCDALLH 100
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 339-452 3.48e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283  339 EKLQSPPTQG---------SQASINHPNLPGQHNVPvshPLNPLQQNHLLPNGlelpfmmmPHPLIPVSLPPASVTMAMS 409
Cdd:pfam03154 422 QQLPPPPAQPpvltqsqslPPPAASHPPTSGLHQVP---SQSPFPQHPFVPGG--------PPPITPPSGPPTSTSSAMP 490

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 971377283  410 QMNHLSTIANMAAAAQVQSPPSRVETSVIKERVPD-------------SPSPAPSL 452
Cdd:pfam03154 491 GIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDeaeepesppppprSPSPEPTV 546
 
Name Accession Description Interval E-value
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 140-234 5.61e-71

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 225.70  E-value: 5.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 140 NECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCK 219
Cdd:cd21081    1 NECKMVEYRGAKVAAFTVDGEELICLPQAFELFLKHLVGGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCK 80

                         90
                 ....*....|....*
gi 971377283 220 LISRKDFETLYNDCT 234
Cdd:cd21081   81 LISRKDFDTLYNDCT 95
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 135-235 4.99e-43

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 150.50  E-value: 4.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283  135 NTPQNNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPG 214
Cdd:pfam02437   2 NTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDF--SLTQINTVCDELIITCVRCTPEQLEILKLLGILPPS 79

                          90       100
                  ....*....|....*....|.
gi 971377283  215 VNRCKLISRKDFETLYNDCTN 235
Cdd:pfam02437  80 VRRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 142-231 4.62e-30

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. Members of this family include the Ski protein, Ski-like protein (Sno), and Dachshund proteins. Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development.


Pssm-ID: 410781  Cd Length: 88  Bit Score: 113.54  E-value: 4.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 142 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVggLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 221
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFV--QTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLI 78

                         90
                 ....*....|
gi 971377283 222 SRKDFETLYN 231
Cdd:cd21074   79 SKSDAERLLN 88
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 142-233 5.01e-10

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar proteins; SKIDA1 is also known as protein DLN-1. Its biological function remains unclear. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410785  Cd Length: 91  Bit Score: 56.58  E-value: 5.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 142 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGlhTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 221
Cdd:cd21082    1 CGREEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRT--TVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLI 78

                         90
                 ....*....|..
gi 971377283 222 SRKDFETLYNDC 233
Cdd:cd21082   79 SREDVERLYSSY 90
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 139-231 2.16e-06

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410787  Cd Length: 100  Bit Score: 46.49  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 139 NNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRC 218
Cdd:cd21084    5 STELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSC 82

                         90
                 ....*....|...
gi 971377283 219 KLISRKDFETLYN 231
Cdd:cd21084   83 GLITLTDAQRLCN 95
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 142-229 4.24e-06

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and similar proteins; Skor1, also known as functional Smad-suppressing element on chromosome 15 (Fussel-15), LBX1 corepressor 1, or ladybird homeobox corepressor 1, acts as a transcriptional corepressor of LBX1 and inhibits BMP signaling. Skor2, also known as functional Smad-suppressing element on chromosome 18 (Fussel-18), LBX1 corepressor 1-like protein, or ladybird homeobox corepressor 1-like protein, exhibits transcriptional repressor activity. It acts as a transforming growth factor-beta (TGF-beta) antagonist in the nervous system. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410783  Cd Length: 91  Bit Score: 45.51  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 142 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 221
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDY--SYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMI 78


                 ....*...
gi 971377283 222 SRKDFETL 229
Cdd:cd21080   79 TKREAERL 86
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 142-231 1.89e-04

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410782  Cd Length: 91  Bit Score: 40.63  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 142 CKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 221
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDF--SLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLI 78

                         90
                 ....*....|
gi 971377283 222 SRKDFETLYN 231
Cdd:cd21079   79 TKTDAERLCS 88
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 142-231 8.27e-04

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410786  Cd Length: 102  Bit Score: 39.28  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283 142 CKMVdLRGAKVASFTVEGCELICLPQAFDLFLKHLvgGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLI 221
Cdd:cd21083   11 CETI-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLI 87

                         90
                 ....*....|
gi 971377283 222 SRKDFETLYN 231
Cdd:cd21083   88 TKTDAERLCN 97
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 339-452 3.48e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971377283  339 EKLQSPPTQG---------SQASINHPNLPGQHNVPvshPLNPLQQNHLLPNGlelpfmmmPHPLIPVSLPPASVTMAMS 409
Cdd:pfam03154 422 QQLPPPPAQPpvltqsqslPPPAASHPPTSGLHQVP---SQSPFPQHPFVPGG--------PPPITPPSGPPTSTSSAMP 490

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 971377283  410 QMNHLSTIANMAAAAQVQSPPSRVETSVIKERVPD-------------SPSPAPSL 452
Cdd:pfam03154 491 GIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDeaeepesppppprSPSPEPTV 546
 
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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