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Conserved domains on  [gi|1585770995|ref|XP_028080295|]
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actin-depolymerizing factor 5-like [Camellia sinensis]

Protein Classification

actin-depolymerizing factor 5( domain architecture ID 10791535)

actin-depolymerizing factor 5 (ADF-5) participates in drought stress by regulating stomatal closure, and may also serve as a potential downstream target of the drought stress/ABA signaling pathway via members of the ABF/AREB transcription factors family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 42-182 2.58e-107

actin depolymerizing factor; Provisional


:

Pssm-ID: 178755  Cd Length: 141  Bit Score: 303.00  E-value: 2.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  42 MAFKMATTGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVD 121
Cdd:PLN03216    1 MAFKMATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585770995 122 NCRKSKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRAQ 182
Cdd:PLN03216   81 NCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 42-182 2.58e-107

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 303.00  E-value: 2.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  42 MAFKMATTGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVD 121
Cdd:PLN03216    1 MAFKMATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585770995 122 NCRKSKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRAQ 182
Cdd:PLN03216   81 NCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 49-181 2.91e-60

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: 183.53  E-value: 2.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  49 TGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVDNCRKSKI 128
Cdd:cd11286     1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585770995 129 FFIAWAPTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRA 181
Cdd:cd11286    81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 55-181 7.21e-49

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 154.75  E-value: 7.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995   55 EECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTvDNCRKSKIFFIAWA 134
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1585770995  135 PTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRA 181
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKL 126
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 57-179 2.61e-45

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 145.41  E-value: 2.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  57 CKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWAPT 136
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1585770995 137 ASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKD 179
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 42-182 2.58e-107

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 303.00  E-value: 2.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  42 MAFKMATTGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVD 121
Cdd:PLN03216    1 MAFKMATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585770995 122 NCRKSKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRAQ 182
Cdd:PLN03216   81 NCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRAK 141
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 49-181 2.91e-60

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: 183.53  E-value: 2.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  49 TGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVDNCRKSKI 128
Cdd:cd11286     1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585770995 129 FFIAWAPTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRA 181
Cdd:cd11286    81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 55-181 7.21e-49

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 154.75  E-value: 7.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995   55 EECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTvDNCRKSKIFFIAWA 134
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1585770995  135 PTASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKDRA 181
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKL 126
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 57-179 2.61e-45

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 145.41  E-value: 2.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  57 CKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDKVGGPGESYDDLTASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWAPT 136
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1585770995 137 ASRIRAKVLYATSKDGLRRVLDGIHYEVQATDPTEMGIDVIKD 179
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 71-168 3.91e-20

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: 80.20  E-value: 3.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  71 KYIVFKIDEGSRLVtvdKVGGPGESY-DDLTASLPTDDCRYAVFDFDFVTVDNCRkSKIFFIAWAPTASRIRAKVLYATS 149
Cdd:cd00013     1 DWVLFKVDAKKEEI---VVGSTGAGFlDEFLEELPEDDPRYAFYRFKYPHSDDKR-SKFVFISWIPDGVSIKQKMVYATN 76

                          90
                  ....*....|....*....
gi 1585770995 150 KDGLRRVLDGIHYEVQATD 168
Cdd:cd00013    77 KQTLKEALFGLAVPVQIRD 95
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 49-160 1.42e-15

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 69.21  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  49 TGMWVTEECKNSFMEMKWKKVHKYIVFKIDEGSRLVTVDkvgGPGESYDDLTASLPTDD---CRYAVFDfdfvtvdncRK 125
Cdd:PTZ00152    3 SGIRVNDNCVTEFNNMKIRKTCRWIIFVIENCEIIIHSK---GATTTLTELVGSIDKNDkiqCAYVVFD---------AV 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1585770995 126 SKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDGI 160
Cdd:PTZ00152   71 NKIHFFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 42-179 3.06e-10

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: 55.32  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  42 MAFKMattgmwvTEECKNSFMEMKwKKVHKYIVFKIDEGSRLVTVDKVGgPGESYDDLTASLPTDDCRYAVFDFDfvtvd 121
Cdd:cd11284     3 VAFPV-------SEEAKDALSELA-SGGVNLVQLSIDLENETIELVSSS-SISIPDDLSSLIPSDHPRYHFYRYP----- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585770995 122 NCRKSKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDG-----IHYEVQATDPTEMGIDVIKD 179
Cdd:cd11284    69 HTYLSSVVFIYSCPSGSKVKERMLYASSKSGLLNHAEDegkieIDKKIEIGDPDELTESFLSD 131
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 73-158 1.71e-08

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: 50.31  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  73 IVFKIDEGSRLVTVDKVGgPGESYDDLTASLPTDDCRYAVFDFDFVTVDNcRKS-KIFFIAWAPTASRIRAKVLYATSKD 151
Cdd:cd11283    24 LILKIDKEKQEIVVDEEL-EDISIEELAEELPEHSPRFVLYSYKMKHDDG-RISyPLVLIYWSPQGCSPELQMLYAGAKE 101


                  ....*..
gi 1585770995 152 GLRRVLD 158
Cdd:cd11283   102 LLVKEAE 108
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 125-172 1.70e-04

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: 39.92  E-value: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1585770995 125 KSKIFFIAWAPTASRIRAKVLYATSKDGLRRVLDGIH--YEVQATDPTEM 172
Cdd:cd11285    77 GYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSNHikDELFATELEEL 126
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 72-172 5.72e-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: 38.00  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585770995  72 YIVFKIDEGSRLVtvdkVGGPGESY-DDLTASLPTDDCRYAVFDFDFvTVDNCRKSKIFFIAWAPTASRIRAKVLYATSK 150
Cdd:cd11282    18 WVLLGYESSNTLV----LRGSGSGGiDELKAQLPDDEVLFGYVRITL-GDGESKRSKFVFITWIGENVSVLRRAKVSVHK 92

                          90       100
                  ....*....|....*....|..
gi 1585770995 151 DGLRRVLDGIHYEVQATDPTEM 172
Cdd:cd11282    93 GDVKEVLSPFHVELTASSKDEL 114
 
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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