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Conserved domains on  [gi|2006345073|ref|XP_039942308|]
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trafficking protein particle complex subunit 3 isoform X1 [Hirundo rustica]

Protein Classification

BET3 family protein( domain architecture ID 10202206)

BET3 family protein such as trafficking protein particle complex subunit 3 (BET3), a component of the multisubunit transport protein particle (TRAPP) complex that may play a role in vesicular transport from endoplasmic reticulum to Golgi

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRAPPC3_bet3 cd14942
Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the ...
 31-185 1.26e-113

Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the trafficking protein particle complex (TRAPP). Bet3 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPC3 has also been shown to be additionally important for membrane fusion during the formation of vesicular tubular clusters (VTC). In its core, Bet3 forms a hydrophobic channel that also contains a conserved acylation site.


:

Pssm-ID: 271345  Cd Length: 155  Bit Score: 320.23  E-value: 1.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  31 NSELFTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSIT 110
Cdd:cd14942     1 NAELFTLTYGALVAQLLKDYEDVEEVNKQLDKMGYNIGVRLIEEFLAKSGVGRCKDFRETAEVIAKVAFKMFLGVTAEVT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006345073 111 NWSPGGDEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQMAVDVKFVQDTLKGDSVTEIRMKFIR 185
Cdd:cd14942    81 NWSSDGDEFSLILEENPLADFVELPPELSGLWYSNILCGVIRGALEMVQMRVEVTFVQDTLRGDDVTEIRVKLIE 155
 
Name Accession Description Interval E-value
TRAPPC3_bet3 cd14942
Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the ...
 31-185 1.26e-113

Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the trafficking protein particle complex (TRAPP). Bet3 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPC3 has also been shown to be additionally important for membrane fusion during the formation of vesicular tubular clusters (VTC). In its core, Bet3 forms a hydrophobic channel that also contains a conserved acylation site.


Pssm-ID: 271345  Cd Length: 155  Bit Score: 320.23  E-value: 1.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  31 NSELFTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSIT 110
Cdd:cd14942     1 NAELFTLTYGALVAQLLKDYEDVEEVNKQLDKMGYNIGVRLIEEFLAKSGVGRCKDFRETAEVIAKVAFKMFLGVTAEVT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006345073 111 NWSPGGDEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQMAVDVKFVQDTLKGDSVTEIRMKFIR 185
Cdd:cd14942    81 NWSSDGDEFSLILEENPLADFVELPPELSGLWYSNILCGVIRGALEMVQMRVEVTFVQDTLRGDDVTEIRVKLIE 155
TRAPP pfam04051
Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or ...
 35-180 1.34e-62

Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or fusion of ER-to-Golgi transport vesicles with their acceptor compartment. TRAPP is a large multimeric protein that contains at least 10 subunits. This family contains many TRAPP family proteins. The Bet3 subunit is one of the better characterized TRAPP proteins and has a dimeric structure with hydrophobic channels. The channel entrances are located on a putative membrane-interacting surface that is distinctively flat, wide and decorated with positively charged residues. Bet3 is proposed to localize TRAPP to the Golgi.


Pssm-ID: 461147  Cd Length: 148  Bit Score: 190.76  E-value: 1.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  35 FTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSP 114
Cdd:pfam04051   1 FALLYGELVAYLQKDSEDVEEVNKRLEKMGYNIGQRLIELFLARDSRCRFTDFLETLKFICKDVWKMLFGKQADNLETNH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006345073 115 GGdEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQM--AVDVKFV-QDTLKGDSVTEIR 180
Cdd:pfam04051  81 DG-EYVLIDNEPPLTRFVELPKDGSQLNYLAFLCGIIRGALEMLGFpaRVTAHFVpSDVLRGDTTFEIK 148
COG5128 COG5128
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
17-155 1.94e-05

Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];


Pssm-ID: 227457  Cd Length: 208  Bit Score: 43.76  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  17 YLPFISPSASLQLMNSEL----FTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEdflaRSNVGRCHDFRET-- 90
Cdd:COG5128    23 LMGKSVYEQNLKIMKREVplstMAFLFCEMIEYLMEQRSGIQDFEAKLKSIGYEVGIKLLE----LCNFRRRNPKREVri 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  91 ADVIAKVAFKM--YL--GITPSITNWSPGGDEFsLILENNPLVD-FVELPDNHSTLIYSNLLCGVLRGAL 155
Cdd:COG5128    99 LTILQRIHFDLwsYLfgDSDDRLEKSREVDREY-MIVDNDPLLSrFISVPDEWNGLSCDSIVCGIIQGFL 167
 
Name Accession Description Interval E-value
TRAPPC3_bet3 cd14942
Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the ...
 31-185 1.26e-113

Bet3-TRAPPC3 subunit of the TRAPP complex; Bet3 (also known as TRAPPC3) subunit of the trafficking protein particle complex (TRAPP). Bet3 is one of the six core subunits of TRAPP complexes which play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPC3 has also been shown to be additionally important for membrane fusion during the formation of vesicular tubular clusters (VTC). In its core, Bet3 forms a hydrophobic channel that also contains a conserved acylation site.


Pssm-ID: 271345  Cd Length: 155  Bit Score: 320.23  E-value: 1.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  31 NSELFTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSIT 110
Cdd:cd14942     1 NAELFTLTYGALVAQLLKDYEDVEEVNKQLDKMGYNIGVRLIEEFLAKSGVGRCKDFRETAEVIAKVAFKMFLGVTAEVT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006345073 111 NWSPGGDEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQMAVDVKFVQDTLKGDSVTEIRMKFIR 185
Cdd:cd14942    81 NWSSDGDEFSLILEENPLADFVELPPELSGLWYSNILCGVIRGALEMVQMRVEVTFVQDTLRGDDVTEIRVKLIE 155
TRAPPC_bet3-like cd14941
Bet3-like domains of TRAPP; Bet3-like domains of a subfamily of core components of the ...
 31-182 1.28e-78

Bet3-like domains of TRAPP; Bet3-like domains of a subfamily of core components of the trafficking protein particle complex (TRAPP) include TRAPPC3, TRAPPC5, and TRAPPC6A. TRAPP complexes play a key role in the regulation of ER-to-Golgi and intra-Golgi transport by tethering the vesicle membrane to the target membrane. TRAPPs are large multimeric protein complexes which contain six core subunits that belong to two distinct structural families, the bet3-like family and the sedlin-like family.


Pssm-ID: 271344  Cd Length: 152  Bit Score: 231.58  E-value: 1.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  31 NSELFTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSIT 110
Cdd:cd14941     1 SVSLFALLFGEMVSQLCKDYESVGDVNTKLADMGFNIGARLIEDFLARKNGKRCTKVLDILLFIKKNAWKALFGKTPDIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006345073 111 NWSPGGDEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQMAVDVKFVQDTLKGDSVTEIRMK 182
Cdd:cd14941    81 NWSHDDDTYSLIDNEPPLNDFISLPDENSSLNYSAFTCGIIRGILENVGFPCKVTAHWDKLGGDPGTEIMIK 152
TRAPP pfam04051
Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or ...
 35-180 1.34e-62

Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or fusion of ER-to-Golgi transport vesicles with their acceptor compartment. TRAPP is a large multimeric protein that contains at least 10 subunits. This family contains many TRAPP family proteins. The Bet3 subunit is one of the better characterized TRAPP proteins and has a dimeric structure with hydrophobic channels. The channel entrances are located on a putative membrane-interacting surface that is distinctively flat, wide and decorated with positively charged residues. Bet3 is proposed to localize TRAPP to the Golgi.


Pssm-ID: 461147  Cd Length: 148  Bit Score: 190.76  E-value: 1.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  35 FTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSP 114
Cdd:pfam04051   1 FALLYGELVAYLQKDSEDVEEVNKRLEKMGYNIGQRLIELFLARDSRCRFTDFLETLKFICKDVWKMLFGKQADNLETNH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006345073 115 GGdEFSLILENNPLVDFVELPDNHSTLIYSNLLCGVLRGALEMVQM--AVDVKFV-QDTLKGDSVTEIR 180
Cdd:pfam04051  81 DG-EYVLIDNEPPLTRFVELPKDGSQLNYLAFLCGIIRGALEMLGFpaRVTAHFVpSDVLRGDTTFEIK 148
COG5128 COG5128
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
17-155 1.94e-05

Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];


Pssm-ID: 227457  Cd Length: 208  Bit Score: 43.76  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  17 YLPFISPSASLQLMNSEL----FTLTYGALVTQLCKDYENDDDVNKQLDKMGYNIGVRLIEdflaRSNVGRCHDFRET-- 90
Cdd:COG5128    23 LMGKSVYEQNLKIMKREVplstMAFLFCEMIEYLMEQRSGIQDFEAKLKSIGYEVGIKLLE----LCNFRRRNPKREVri 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006345073  91 ADVIAKVAFKM--YL--GITPSITNWSPGGDEFsLILENNPLVD-FVELPDNHSTLIYSNLLCGVLRGAL 155
Cdd:COG5128    99 LTILQRIHFDLwsYLfgDSDDRLEKSREVDREY-MIVDNDPLLSrFISVPDEWNGLSCDSIVCGIIQGFL 167
 
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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