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Conserved domains on  [gi|17367307|sp|Q9ZSK2|]
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RecName: Full=Actin-depolymerizing factor 6; Short=ADF-6; Short=AtADF6

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 11-145 4.96e-69

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member PLN03216:

Pssm-ID: 472830  Cd Length: 141  Bit Score: 204.77  E-value: 4.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307   11 AISGMGVADESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKS 90
Cdd:PLN03216   6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17367307   91 KIFFFAWSPSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERA 145
Cdd:PLN03216  86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 11-145 4.96e-69

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 204.77  E-value: 4.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307   11 AISGMGVADESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKS 90
Cdd:PLN03216   6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17367307   91 KIFFFAWSPSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERA 145
Cdd:PLN03216  86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 13-145 1.50e-64

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 193.16  E-value: 1.50e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  13 SGMGVADESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKSKI 92
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17367307  93 FFFAWSPSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERA 145
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-146 8.61e-52

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 160.53  E-value: 8.61e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307     19 DESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTsENCQKSKIFFFAWS 98
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17367307     99 PSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERAN 146
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 22-143 1.09e-49

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 155.04  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307    22 KTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKSKIFFFAWSPST 101
Cdd:pfam00241   2 KEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPDG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17367307   102 SGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRE 143
Cdd:pfam00241  82 APIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 11-145 4.96e-69

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 204.77  E-value: 4.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307   11 AISGMGVADESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKS 90
Cdd:PLN03216   6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17367307   91 KIFFFAWSPSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERA 145
Cdd:PLN03216  86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 13-145 1.50e-64

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 193.16  E-value: 1.50e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  13 SGMGVADESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKSKI 92
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17367307  93 FFFAWSPSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERA 145
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-146 8.61e-52

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 160.53  E-value: 8.61e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307     19 DESKTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTsENCQKSKIFFFAWS 98
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17367307     99 PSTSGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRERAN 146
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 22-143 1.09e-49

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 155.04  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307    22 KTTFLELQRKKTHRYVVFKIDESKKEVVVEKTGNPTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKSKIFFFAWSPST 101
Cdd:pfam00241   2 KEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPDG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17367307   102 SGIRAKVLYSTSKDQLSRELQGIHYEIQATDPTEVDLEVLRE 143
Cdd:pfam00241  82 APIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 35-132 3.47e-25

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


Pssm-ID: 200435  Cd Length: 97  Bit Score: 92.14  E-value: 3.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  35 RYVVFKIDESKKEVVVEKTGNPTEsyDDFLASLPDNDCRYAVYDFDFVTSENcQKSKIFFFAWSPSTSGIRAKVLYSTSK 114
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAGFL--DEFLEELPEDDPRYAFYRFKYPHSDD-KRSKFVFISWIPDGVSIKQKMVYATNK 77

                        90
                ....*....|....*...
gi 17367307 115 DQLSRELQGIHYEIQATD 132
Cdd:cd00013  78 QTLKEALFGLAVPVQIRD 95
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 12-124 1.85e-18

cofilin/actin-depolymerizing factor 1-like protein; Provisional


Pssm-ID: 173441  Cd Length: 122  Bit Score: 75.76  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307   12 ISGMGVADESKTTFLELQRKKTHRYVVFKIDESkkEVVVEKTGNPTeSYDDFLASLPDND---CRYAVYDfdfvtsencQ 88
Cdd:PTZ00152   2 ISGIRVNDNCVTEFNNMKIRKTCRWIIFVIENC--EIIIHSKGATT-TLTELVGSIDKNDkiqCAYVVFD---------A 69

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 17367307   89 KSKIFFFAWSPSTSGIRAKVLYSTSKDQLSRELQGI 124
Cdd:PTZ00152  70 VNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 14-143 3.09e-12

C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200440  Cd Length: 132  Bit Score: 59.55  E-value: 3.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  14 GMGVADESKTTFLELQRKKtHRYVVFKIDESKKEVVVEKTGNpTESYDDFLASLPDNDCRYAVYDFDfvtseNCQKSKIF 93
Cdd:cd11284   4 AFPVSEEAKDALSELASGG-VNLVQLSIDLENETIELVSSSS-ISIPDDLSSLIPSDHPRYHFYRYP-----HTYLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17367307  94 FFAWSPSTSGIRAKVLYSTSKDQLSRELQG-----IHYEIQATDPTEVDLEVLRE 143
Cdd:cd11284  77 FIYSCPSGSKVKERMLYASSKSGLLNHAEDegkieIDKKIEIGDPDELTESFLSD 131
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 28-122 3.04e-11

ADF-homology domain of glia maturation factor beta and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Most of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The glia maturation factor (GMF), however, does not bind actin but interacts with the Arp2/3 complex (which contains actin-related proteins, amongst others) and suppresses Arp2/3 activity, inducing the dissociation of branched daughter filaments from their mother filaments. This family includes both mammalian GMF isoforms, GMF-beta and GMF-gamma. GMF-beta regulates cellular growth, fission, differentiation and apoptosis. GMF-gamma is important in myeloid cell development and is an important regulator for cell migration and polarity in neutrophils.


Pssm-ID: 200439 [Multi-domain]  Cd Length: 122  Bit Score: 56.86  E-value: 3.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  28 LQRKKTHRYVVFKIDESKKEVVVEKTGNpTESYDDFLASLPDNDCRYAVYDFDFVTSENCQKSKIFFFAWSPSTSGIRAK 107
Cdd:cd11283  15 FRKSKANAALILKIDKEKQEIVVDEELE-DISIEELAEELPEHSPRFVLYSYKMKHDDGRISYPLVLIYWSPQGCSPELQ 93

                        90
                ....*....|....*
gi 17367307 108 VLYSTSKDQLSRELQ 122
Cdd:cd11283  94 MLYAGAKELLVKEAE 108
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 38-139 9.17e-08

N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200441  Cd Length: 139  Bit Score: 48.01  E-value: 9.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  38 VFKIDESKKEVVVEKTGNPTESYDDFLASLP-----DNDCRYAVYDFDfvtsENCQKSKIFFFAWSPSTSGIRAKVLYST 112
Cdd:cd11285  25 AIKITIENEELVPDATIETTGSWEQDFDLLVlplleEKEPCYILYRLD----SKSAGYEWVFISFVPDSAPVRQKMLYAS 100

                        90       100
                ....*....|....*....|....*....
gi 17367307 113 SKDQLSRELQGIH--YEIQATDPTEVDLE 139
Cdd:cd11285 101 TRATLKRELGSNHikDELFATELEELTLE 129
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 43-136 1.16e-04

Coactosin-like members of the ADF homology domain family; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The function of coactosins is not well understood. They appear to interfere with the capping of actin filaments in Dictyostelium, and may not be able to bind monomeric globular actin. A role for coactosins as chaperones stabilizing 5-lipoxygenase (5LO) has been suggested; 5LO plays a crucial role in leukotriene synthesis.


Pssm-ID: 200438  Cd Length: 114  Bit Score: 39.16  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  43 ESKKEVVVEKTGNptESYDDFLASLPDNDCRYAVydFDFVTSENCQK-SKIFFFAWSPSTSGIRAKVLYSTSKDQLSREL 121
Cdd:cd11282  24 ESSNTLVLRGSGS--GGIDELKAQLPDDEVLFGY--VRITLGDGESKrSKFVFITWIGENVSVLRRAKVSVHKGDVKEVL 99

                        90
                ....*....|....*
gi 17367307 122 QGIHYEIQATDPTEV 136
Cdd:cd11282 100 SPFHVELTASSKDEL 114
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 31-144 2.85e-03

ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.


Pssm-ID: 200437  Cd Length: 136  Bit Score: 35.69  E-value: 2.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367307  31 KKTHRYVVFKIDESKKEVVVEKTGNPTesYDDFLASLPDNDCRYAvydFDFVTSENCQKSKIFFFAWSPSTSGIRAKVLY 110
Cdd:cd11281  21 KSSTDWALFTYEGKSNDLKVADTGDGG--LEELVEEFSDGKVQYG---FARVKDPNSGLPKFVLINWCGEGVPDARKGSF 95

                        90       100       110
                ....*....|....*....|....*....|....
gi 17367307 111 STSKDQLSRELQGIHYEIQATDPTEVDLEVLRER 144
Cdd:cd11281  96 ASHVAAVANFLKGAHVQINARSEDDLDEDAILKK 129
 
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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