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Conserved domains on  [gi|1279759478|ref|XP_022922159|]
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actin-depolymerizing factor 2 [Cucurbita moschata]

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 ...
 4-138 1.19e-66

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: 198.61  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   4 AASGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKS 83
Cdd:PLN03216    6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1279759478  84 RIIFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSRS 138
Cdd:PLN03216   86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 4-138 1.19e-66

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 198.61  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   4 AASGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKS 83
Cdd:PLN03216    6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1279759478  84 RIIFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSRS 138
Cdd:PLN03216   86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 6-137 5.57e-66

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: 196.24  E-value: 5.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   6 SGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKSRI 85
Cdd:cd11286     1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1279759478  86 IFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSR 137
Cdd:cd11286    81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEK 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 12-137 1.06e-54

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 167.46  E-value: 1.06e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   12 DDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEEnCQKSRIIFIAWS 91
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTTEE-SKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1279759478   92 PDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSR 137
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEK 125
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 14-136 1.31e-48

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 151.96  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478  14 CKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKSRIIFIAWSPD 93
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1279759478  94 TSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRS 136
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 4-138 1.19e-66

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 198.61  E-value: 1.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   4 AASGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKS 83
Cdd:PLN03216    6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1279759478  84 RIIFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSRS 138
Cdd:PLN03216   86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 6-137 5.57e-66

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: 196.24  E-value: 5.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   6 SGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKSRI 85
Cdd:cd11286     1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1279759478  86 IFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSR 137
Cdd:cd11286    81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEK 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 12-137 1.06e-54

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 167.46  E-value: 1.06e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   12 DDCKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEEnCQKSRIIFIAWS 91
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTTEE-SKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1279759478   92 PDTSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRSR 137
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEK 125
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 14-136 1.31e-48

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 151.96  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478  14 CKLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPSQSYEDFAASLPADECRYAVYDFDFVTEENCQKSRIIFIAWSPD 93
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1279759478  94 TSRVRSKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVIRS 136
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 28-125 3.19e-22

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: 84.44  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478  28 RFIVFKIEEKQKQVVVEKLGEPSQsyEDFAASLPADECRYAVYDFDFVTEENcQKSRIIFIAWSPDTSRVRSKMIYASSK 107
Cdd:cd00013     1 DWVLFKVDAKKEEIVVGSTGAGFL--DEFLEELPEDDPRYAFYRFKYPHSDD-KRSKFVFISWIPDGVSIKQKMVYATNK 77

                          90
                  ....*....|....*...
gi 1279759478 108 DRFKRELDGIQVELQATD 125
Cdd:cd00013    78 QTLKEALFGLAVPVQIRD 95
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 5-119 7.74e-20

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 78.84  E-value: 7.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   5 ASGMAVHDDCKLRFLDLKAKRTYRFIVFKIEekQKQVVVEKLGEpSQSYEDFAASLPAD---ECRYAVYDfdfvteencQ 81
Cdd:PTZ00152    2 ISGIRVNDNCVTEFNNMKIRKTCRWIIFVIE--NCEIIIHSKGA-TTTLTELVGSIDKNdkiQCAYVVFD---------A 69

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1279759478  82 KSRIIFIAWSPDTSRVRSKMIYASSKDRFKRELDGIQV 119
Cdd:PTZ00152   70 VNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNV 107
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 6-132 5.70e-15

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: 66.89  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478   6 SGMAVHDDCKLRFLDLKAKRTYRFIVFKIEEKQKQVV--VEKLGEPSQSYEDFAAS-LPADECRYAVYdfdfVTEENCQK 82
Cdd:cd11285     2 SGITASEELLDAFKSAKSSGSVRAIKITIENEELVPDatIETTGSWEQDFDLLVLPlLEEKEPCYILY----RLDSKSAG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1279759478  83 SRIIFIAWSPDTSRVRSKMIYASSKDRFKRELDG--IQVELQATDPTEMGLD 132
Cdd:cd11285    78 YEWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTLE 129
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 15-115 6.90e-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: 55.71  E-value: 6.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478  15 KLRFLDLKAKRTYRFIVFKIEEKQKQVVVEKLGEPsQSYEDFAASLPADECRYAVYDFDFVTEENCQKSRIIFIAWSPDT 94
Cdd:cd11283     9 ALKKFRFRKSKANAALILKIDKEKQEIVVDEELED-ISIEELAEELPEHSPRFVLYSYKMKHDDGRISYPLVLIYWSPQG 87

                          90       100
                  ....*....|....*....|.
gi 1279759478  95 SRVRSKMIYASSKDRFKRELD 115
Cdd:cd11283    88 CSPELQMLYAGAKELLVKEAE 108
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 29-136 6.78e-09

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: 50.69  E-value: 6.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279759478  29 FIVFKIEEKQKQVVVEKlGEPSQSYEDFAASLPADECRYAVYDFDfvteeNCQKSRIIFIAWSPDTSRVRSKMIYASSKD 108
Cdd:cd11284    25 LVQLSIDLENETIELVS-SSSISIPDDLSSLIPSDHPRYHFYRYP-----HTYLSSVVFIYSCPSGSKVKERMLYASSKS 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1279759478 109 RFKREL---DGIQVE--LQATDPTEMGLDVIRS 136
Cdd:cd11284    99 GLLNHAedeGKIEIDkkIEIGDPDELTESFLSD 131
 
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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