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Conserved domains on  [gi|2042456213|emb|CAF4785449|]
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unnamed protein product [Rotaria magnacalcarata]

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 ...
 1-113 1.73e-78

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: 228.03  E-value: 1.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:cd11287     9 MIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPVDDAQELLQ 88

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTN 113
Cdd:cd11287    89 DRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
 
Name Accession Description Interval E-value
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 1-113 1.73e-78

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: 228.03  E-value: 1.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:cd11287     9 MIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPVDDAQELLQ 88

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTN 113
Cdd:cd11287    89 DRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
PLN00162 PLN00162
transport protein sec23; Provisional
 1-145 1.18e-77

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 244.46  E-value: 1.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:PLN00162  618 MIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIK 697

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTNYGwGQGAGAPILTDDVNLQTFMEHLKKLAVSS 145
Cdd:PLN00162  698 ERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSAN-AMGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
1-146 6.68e-64

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 207.81  E-value: 6.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:COG5047   612 MIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQ 691

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTNYgwGQGAGAPILTDDVNLQTFMEHLKKLAVSST 146
Cdd:COG5047   692 DRFPIPRFIVTEQGGSQARFLLSKINPSDITNKM--SGGGSETILTDDVNLQKFMNHLRKLAVSKS 755
Gelsolin pfam00626
Gelsolin repeat;
15-101 1.75e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213  15 PEPVLLDSSSILPDRILLMDTfyhiliyhGETIAQWVKAGYQelPEYENFKQLLQAPVgdateILQNRFPMPRYITTEAG 94
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSS--LLEKLFAALLAAQL-----DDDERFPLPEVIRVPQG 69


                  ....*..
gi 2042456213  95 GSQARFL 101
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 ...
 1-113 1.73e-78

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: 228.03  E-value: 1.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:cd11287     9 MIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPVDDAQELLQ 88

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTN 113
Cdd:cd11287    89 DRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
PLN00162 PLN00162
transport protein sec23; Provisional
 1-145 1.18e-77

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 244.46  E-value: 1.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:PLN00162  618 MIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIK 697

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTNYGwGQGAGAPILTDDVNLQTFMEHLKKLAVSS 145
Cdd:PLN00162  698 ERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSAN-AMGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
1-146 6.68e-64

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 207.81  E-value: 6.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   1 MIQPILYAYSFSGPPEPVLLDSSSILPDRILLMDTFYHILIYHGETIAQWVKAGYQELPEYENFKQLLQAPVGDATEILQ 80
Cdd:COG5047   612 MIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQ 691

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2042456213  81 NRFPMPRYITTEAGGSQARFLLYKVNPSQTHTNYgwGQGAGAPILTDDVNLQTFMEHLKKLAVSST 146
Cdd:COG5047   692 DRFPIPRFIVTEQGGSQARFLLSKINPSDITNKM--SGGGSETILTDDVNLQKFMNHLRKLAVSKS 755
Gelsolin pfam00626
Gelsolin repeat;
15-101 1.75e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213  15 PEPVLLDSSSILPDRILLMDTfyhiliyhGETIAQWVKAGYQelPEYENFKQLLQAPVgdateILQNRFPMPRYITTEAG 94
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSS--LLEKLFAALLAAQL-----DDDERFPLPEVIRVPQG 69


                  ....*..
gi 2042456213  95 GSQARFL 101
Cdd:pfam00626  70 KEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 3-101 2.06e-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: 58.92  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042456213   3 QPILYAYSFSG--PPEPVLLDSSSILPDRILLMDTFYHILIYHGEtiaqwvkagyqelpeyENFKQLLQAPVGDATEILQ 80
Cdd:cd11280     1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64

                          90       100
                  ....*....|....*....|.
gi 2042456213  81 NRFPMPRYITTEAGGSQARFL 101
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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