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Conserved domains on  [gi|2010790805|emb|CAF3722006|]
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unnamed protein product [Rotaria sp. Silwood1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 9-129 8.48e-83

C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.


:

Pssm-ID: 200443 [Multi-domain]  Cd Length: 121  Bit Score: 239.58  E-value: 8.48e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   9 EDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQLLQAPV 88
Cdd:cd11287     1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2010790805  89 GDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTN 129
Cdd:cd11287    81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
 
Name Accession Description Interval E-value
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 9-129 8.48e-83

C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.


Pssm-ID: 200443 [Multi-domain]  Cd Length: 121  Bit Score: 239.58  E-value: 8.48e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   9 EDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQLLQAPV 88
Cdd:cd11287     1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2010790805  89 GDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTN 129
Cdd:cd11287    81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
PLN00162 PLN00162
transport protein sec23; Provisional
 9-161 2.61e-80

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 252.17  E-value: 2.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   9 EDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQLLQAPV 88
Cdd:PLN00162  610 ENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQ 689

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010790805  89 GDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTNfGWGQAVGAPILTDDVNLQTFMEHLKKLAVSS 161
Cdd:PLN00162  690 ADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNS-ANAMGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
3-162 8.92e-69

Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 221.68  E-value: 8.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   3 RHYLLVEDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQ 82
Cdd:COG5047   598 RHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKE 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805  83 LLQAPVGDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTNFGWGQAvgAPILTDDVNLQTFMEHLKKLAVSST 162
Cdd:COG5047   678 LLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGS--ETILTDDVNLQKFMNHLRKLAVSKS 755
Gelsolin pfam00626
Gelsolin repeat;
31-117 3.30e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805  31 PEPVLLDSSSILPDRILLMDTfyhiliyhGETIAQWFkaGYQDLPEYENFKQLLQAPVgdateILQNRFPMPRYIVTEAG 110
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDN--------GFTIFLWV--GKGSSLLEKLFAALLAAQL-----DDDERFPLPEVIRVPQG 69


                  ....*..
gi 2010790805 111 GSQARFL 117
Cdd:pfam00626  70 KEPARFL 76
 
Name Accession Description Interval E-value
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 9-129 8.48e-83

C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.


Pssm-ID: 200443 [Multi-domain]  Cd Length: 121  Bit Score: 239.58  E-value: 8.48e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   9 EDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQLLQAPV 88
Cdd:cd11287     1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2010790805  89 GDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTN 129
Cdd:cd11287    81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
PLN00162 PLN00162
transport protein sec23; Provisional
 9-161 2.61e-80

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 252.17  E-value: 2.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   9 EDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQLLQAPV 88
Cdd:PLN00162  610 ENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQ 689

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010790805  89 GDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTNfGWGQAVGAPILTDDVNLQTFMEHLKKLAVSS 161
Cdd:PLN00162  690 ADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNS-ANAMGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
3-162 8.92e-69

Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 221.68  E-value: 8.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805   3 RHYLLVEDLTQCLVMIQPILYAYSFNGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWFKAGYQDLPEYENFKQ 82
Cdd:COG5047   598 RHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKE 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805  83 LLQAPVGDATEILQNRFPMPRYIVTEAGGSQARFLLYKVNPSQTHTNFGWGQAvgAPILTDDVNLQTFMEHLKKLAVSST 162
Cdd:COG5047   678 LLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGS--ETILTDDVNLQKFMNHLRKLAVSKS 755
Gelsolin pfam00626
Gelsolin repeat;
31-117 3.30e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805  31 PEPVLLDSSSILPDRILLMDTfyhiliyhGETIAQWFkaGYQDLPEYENFKQLLQAPVgdateILQNRFPMPRYIVTEAG 110
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDN--------GFTIFLWV--GKGSSLLEKLFAALLAAQL-----DDDERFPLPEVIRVPQG 69


                  ....*..
gi 2010790805 111 GSQARFL 117
Cdd:pfam00626  70 KEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 19-117 1.36e-12

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.07  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010790805  19 QPILYAYSFNG--PPEPVLLDSSSILPDRILLMDTFYHILIYHGEtiaqwfkagyqdlpeyENFKQLLQAPVGDATEILQ 96
Cdd:cd11280     1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64

                          90       100
                  ....*....|....*....|.
gi 2010790805  97 NRFPMPRYIVTEAGGSQARFL 117
Cdd:cd11280    65 ERKGKPEIVRIRQGQEPREFW 85
 
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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