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Conserved domains on  [gi|19920586|ref|NP_608693|]
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Actin-related protein 2/3 complex, subunit 5, isoform A [Drosophila melanogaster]

Protein Classification

actin-related protein 2/3 complex subunit 5 family protein( domain architecture ID 10520192)

actin-related protein 2/3 complex subunit 5 (ARPC5) family protein similar to ARPC5, a component of the Arp2/3 complex that mediates actin polymerization upon stimulation by nucleation-promoting factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P16-Arc pfam04699
ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the ...
 9-147 5.20e-71

ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the control of actin polymerization. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. The precise function of p16-Arc is currently unknown. Its structure consists of a single domain containing a bundle of seven alpha helices.


:

Pssm-ID: 461399  Cd Length: 146  Bit Score: 210.06  E-value: 5.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920586     9 AFRKIDVDQYNEDNFREDD------GVESAAAGPDESEITTLLTQGKSVEALLSALQNAPLRCKNQNVKDHALNITLRVL 82
Cdd:pfam04699   1 DFRKIDIDAYDPDSFTEEDlypppsEVSLAEAQPLASQVRSLLSSGDAEGALKLALDNPPYGADEQAAKDLHLQTVLEVL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920586    83 LSIKSTQMDQAIDTLDQnDLIDVLMKYIYRGFEIPSEGSSGHLLQWHEKAFAKGGVGCIVRVLSD 147
Cdd:pfam04699  81 SSIKSSDITNIVKSLDS-EQQDVLMKYLYKGMSLPSEKSGSVLLSWHEKLVEVAGVGCIVRVLTD 144
 
Name Accession Description Interval E-value
P16-Arc pfam04699
ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the ...
 9-147 5.20e-71

ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the control of actin polymerization. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. The precise function of p16-Arc is currently unknown. Its structure consists of a single domain containing a bundle of seven alpha helices.


Pssm-ID: 461399  Cd Length: 146  Bit Score: 210.06  E-value: 5.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920586     9 AFRKIDVDQYNEDNFREDD------GVESAAAGPDESEITTLLTQGKSVEALLSALQNAPLRCKNQNVKDHALNITLRVL 82
Cdd:pfam04699   1 DFRKIDIDAYDPDSFTEEDlypppsEVSLAEAQPLASQVRSLLSSGDAEGALKLALDNPPYGADEQAAKDLHLQTVLEVL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920586    83 LSIKSTQMDQAIDTLDQnDLIDVLMKYIYRGFEIPSEGSSGHLLQWHEKAFAKGGVGCIVRVLSD 147
Cdd:pfam04699  81 SSIKSSDITNIVKSLDS-EQQDVLMKYLYKGMSLPSEKSGSVLLSWHEKLVEVAGVGCIVRVLTD 144
 
Name Accession Description Interval E-value
P16-Arc pfam04699
ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the ...
 9-147 5.20e-71

ARP2/3 complex 16 kDa subunit (p16-Arc); The Arp2/3 protein complex has been implicated in the control of actin polymerization. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. The precise function of p16-Arc is currently unknown. Its structure consists of a single domain containing a bundle of seven alpha helices.


Pssm-ID: 461399  Cd Length: 146  Bit Score: 210.06  E-value: 5.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920586     9 AFRKIDVDQYNEDNFREDD------GVESAAAGPDESEITTLLTQGKSVEALLSALQNAPLRCKNQNVKDHALNITLRVL 82
Cdd:pfam04699   1 DFRKIDIDAYDPDSFTEEDlypppsEVSLAEAQPLASQVRSLLSSGDAEGALKLALDNPPYGADEQAAKDLHLQTVLEVL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920586    83 LSIKSTQMDQAIDTLDQnDLIDVLMKYIYRGFEIPSEGSSGHLLQWHEKAFAKGGVGCIVRVLSD 147
Cdd:pfam04699  81 SSIKSSDITNIVKSLDS-EQQDVLMKYLYKGMSLPSEKSGSVLLSWHEKLVEVAGVGCIVRVLTD 144
 
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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