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Conserved domains on  [gi|1720380300|ref|XP_030103770|]
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glia maturation factor beta isoform X2 [Mus musculus]

Protein Classification

glia maturation factor( domain architecture ID 10181677)

glia maturation factor interacts with the Arp2/3 complex and suppresses Arp2/3 activity, inducing the dissociation of branched daughter filaments from their mother filaments.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 1-98 1.94e-53

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: 162.79  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLV 80
Cdd:cd11283    26 LKIDKEKQEIVVDEELEDISIEELAEELPEHSPR-FVLYSYKMKHDDGRISYPLVLIYWSPQGCSPELQMLYAGAKELLV 104

                          90
                  ....*....|....*...
gi 1720380300  81 QTAELTKVFEIRNTEDLT 98
Cdd:cd11283   105 KEAEVTKVFEIRDGEELT 122
 
Name Accession Description Interval E-value
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 1-98 1.94e-53

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: 162.79  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLV 80
Cdd:cd11283    26 LKIDKEKQEIVVDEELEDISIEELAEELPEHSPR-FVLYSYKMKHDDGRISYPLVLIYWSPQGCSPELQMLYAGAKELLV 104

                          90
                  ....*....|....*...
gi 1720380300  81 QTAELTKVFEIRNTEDLT 98
Cdd:cd11283   105 KEAEVTKVFEIRDGEELT 122
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1-107 1.01e-32

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 110.84  E-value: 1.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300    1 MKIDKDERLVVLDEE-LEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLcFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:smart00102  21 FKIDKDNEEIVVEEVgSTEDSYDEFVEELPEDECR-YALYDYKFTTEESKKSKIV-FIFWSPDGAPVKSKMLYASSKDTL 98

                           90       100
                   ....*....|....*....|....*....
gi 1720380300   80 VQTAELTKV-FEIRNTEDLTEEWLREKLG 107
Cdd:smart00102  99 KKELGGIQVeVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1-104 1.56e-31

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 107.66  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEG-VSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:pfam00241  19 FKIDDDKEEIVVEETGEGgLSYDEFLEELPDDEPR-YAVYRFEYTHDDGSKRSKLVFITWCPDGAPIKRKMLYASSKAAL 97

                          90       100
                  ....*....|....*....|....*.
gi 1720380300  80 VQTAE-LTKVFEIRNTEDLTEEWLRE 104
Cdd:pfam00241  98 KRELKgIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 2-79 7.04e-04

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 36.83  E-value: 7.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380300   2 KIDKDERLVVLDE-ELEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:PLN03216   35 KIDEKSRKVTVDKvGGPGESYDDLAASLPTDDCR-YAVFDFDFVTVDNCRKSKIFFIAWSPEASRIRAKMLYATSKDGL 112
 
Name Accession Description Interval E-value
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 1-98 1.94e-53

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: 162.79  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLV 80
Cdd:cd11283    26 LKIDKEKQEIVVDEELEDISIEELAEELPEHSPR-FVLYSYKMKHDDGRISYPLVLIYWSPQGCSPELQMLYAGAKELLV 104

                          90
                  ....*....|....*...
gi 1720380300  81 QTAELTKVFEIRNTEDLT 98
Cdd:cd11283   105 KEAEVTKVFEIRDGEELT 122
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1-107 1.01e-32

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 110.84  E-value: 1.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300    1 MKIDKDERLVVLDEE-LEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLcFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:smart00102  21 FKIDKDNEEIVVEEVgSTEDSYDEFVEELPEDECR-YALYDYKFTTEESKKSKIV-FIFWSPDGAPVKSKMLYASSKDTL 98

                           90       100
                   ....*....|....*....|....*....
gi 1720380300   80 VQTAELTKV-FEIRNTEDLTEEWLREKLG 107
Cdd:smart00102  99 KKELGGIQVeVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1-104 1.56e-31

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 107.66  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEG-VSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:pfam00241  19 FKIDDDKEEIVVEETGEGgLSYDEFLEELPDDEPR-YAVYRFEYTHDDGSKRSKLVFITWCPDGAPIKRKMLYASSKAAL 97

                          90       100
                  ....*....|....*....|....*.
gi 1720380300  80 VQTAE-LTKVFEIRNTEDLTEEWLRE 104
Cdd:pfam00241  98 KRELKgIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1-95 3.61e-27

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: 95.61  E-value: 3.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSpDELKDELPERQPRtFIVYSYKYQHDDgRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLV 80
Cdd:cd00013     5 FKVDAKKEEIVVGSTGAGFL-DEFLEELPEDDPR-YAFYRFKYPHSD-DKRSKFVFISWIPDGVSIKQKMVYATNKQTLK 81

                          90
                  ....*....|....*.
gi 1720380300  81 QTAE-LTKVFEIRNTE 95
Cdd:cd00013    82 EALFgLAVPVQIRDGD 97
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 1-105 5.76e-18

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: 73.42  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSPDELKDELPERQPR-TFivysYKYQHDDGRVSYplcFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:cd11284    28 LSIDLENETIELVSSSSISIPDDLSSLIPSDHPRyHF----YRYPHTYLSSVV---FIYSCPSGSKVKERMLYASSKSGL 100

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720380300  80 VQTAE------LTKVFEIRNTEDLTEEWLREK 105
Cdd:cd11284   101 LNHAEdegkieIDKKIEIGDPDELTESFLSDE 132
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 1-106 7.36e-15

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: 65.27  E-value: 7.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380300   1 MKIDKDERLVVLDEELEGVSP-DELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:cd11286    27 FKISDDKKEIVVEKVGERDASyDDFLEKLPENECR-YAVYDFEYETKDGGKRSKLVFISWCPDTAPIKSKMLYASSKDAL 105

                          90       100
                  ....*....|....*....|....*...
gi 1720380300  80 VQT-AELTKVFEIRNTEDLTEEWLREKL 106
Cdd:cd11286   106 KKKlNGIKKEIQATDLSELSEEEILEKL 133
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 2-79 7.04e-04

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 36.83  E-value: 7.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380300   2 KIDKDERLVVLDE-ELEGVSPDELKDELPERQPRtFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKL 79
Cdd:PLN03216   35 KIDEKSRKVTVDKvGGPGESYDDLAASLPTDDCR-YAVFDFDFVTVDNCRKSKIFFIAWSPEASRIRAKMLYATSKDGL 112
 
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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