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Conserved domains on  [gi|1936209118|gb|KAF9609302|]
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hypothetical protein IFM89_015547 [Coptis chinensis]

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 ...
 42-105 3.43e-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.


The actual alignment was detected with superfamily member PLN03216:

Pssm-ID: 472830  Cd Length: 141  Bit Score: 84.98  E-value: 3.43e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISWRKTREK 105
Cdd:PLN03216   35 KIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWSPEASR 98
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 42-105 3.43e-22

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 84.98  E-value: 3.43e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISWRKTREK 105
Cdd:PLN03216   35 KIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWSPEASR 98
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 42-99 1.46e-19

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: 77.60  E-value: 1.46e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISW 99
Cdd:cd11286    28 KISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVFISW 85
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 42-99 1.31e-14

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 65.00  E-value: 1.31e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118   42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTsENCQKSKVFFISW 99
Cdd:smart00102  22 KIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFW 78
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 42-99 3.08e-14

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 63.75  E-value: 3.08e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISW 99
Cdd:pfam00241  20 KIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITW 77
 
Name Accession Description Interval E-value
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 42-105 3.43e-22

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 84.98  E-value: 3.43e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISWRKTREK 105
Cdd:PLN03216   35 KIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWSPEASR 98
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 42-99 1.46e-19

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: 77.60  E-value: 1.46e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISW 99
Cdd:cd11286    28 KISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVFISW 85
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 42-99 1.31e-14

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 65.00  E-value: 1.31e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118   42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTsENCQKSKVFFISW 99
Cdd:smart00102  22 KIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFW 78
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 42-99 3.08e-14

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 63.75  E-value: 3.08e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118  42 KLDLRKREVVVEKTVDPAENDEDFAASLPENDCRYAVCDFNFVTSENCQKSKVFFISW 99
Cdd:pfam00241  20 KIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITW 77
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 42-99 1.39e-05

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: 40.91  E-value: 1.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936209118  42 KLDLRKREVVVEKTvdPAENDEDFAASLPENDCRYAVCDFNFVTSENcQKSKVFFISW 99
Cdd:cd00013     6 KVDAKKEEIVVGST--GAGFLDEFLEELPEDDPRYAFYRFKYPHSDD-KRSKFVFISW 60
 
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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