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Conserved domains on  [gi|2548884094|pdb|7YH3|C]
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Chain C, TRAPPC3 from Thorarchaeota SMTZ1-45

Protein Classification

trafficking protein particle complex subunit( domain architecture ID 230206)

trafficking protein particle complex subunit is a component of TRAPP (transport protein particle) tethering complexes that have an important role at the different steps of vesicle transport

CATH:  3.30.1380.20
Gene Ontology:  GO:0006888|GO:0030008
PubMed:  9564032|27066478|18801063|22669257|20966969

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRAPP super family cl45956
Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or ...
 14-139 4.29e-06

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.


The actual alignment was detected with superfamily member pfam04051:

Pssm-ID: 461147  Cd Length: 148  Bit Score: 44.00  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C         14 LYSHYVEQILSETNSIDDANQKLRDLGKELGQQIylnteiVE----KTKENVTTRE-EVAKLI-ENVYKVLFDKKPKDVd 87
Cdd:pfam04051   4 LYGELVAYLQKDSEDVEEVNKRLEKMGYNIGQRL------IElflaRDSRCRFTDFlETLKFIcKDVWKMLFGKQADNL- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
7YH3_C         88 mKTARGSVRITDDNCVWCQE-VNL-EGMRGFGYCEIFSGILESILEFKGVDAKV 139
Cdd:pfam04051  77 -ETNHDGEYVLIDNEPPLTRfVELpKDGSQLNYLAFLCGIIRGALEMLGFPARV 129
 
Name Accession Description Interval E-value
TRAPP pfam04051
Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or ...
 14-139 4.29e-06

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: 44.00  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C         14 LYSHYVEQILSETNSIDDANQKLRDLGKELGQQIylnteiVE----KTKENVTTRE-EVAKLI-ENVYKVLFDKKPKDVd 87
Cdd:pfam04051   4 LYGELVAYLQKDSEDVEEVNKRLEKMGYNIGQRL------IElflaRDSRCRFTDFlETLKFIcKDVWKMLFGKQADNL- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
7YH3_C         88 mKTARGSVRITDDNCVWCQE-VNL-EGMRGFGYCEIFSGILESILEFKGVDAKV 139
Cdd:pfam04051  77 -ETNHDGEYVLIDNEPPLTRfVELpKDGSQLNYLAFLCGIIRGALEMLGFPARV 129
COG1719 COG1719
Predicted hydrocarbon binding protein, contains 4VR domain [General function prediction only];
3-159 4.83e-04

Predicted hydrocarbon binding protein, contains 4VR domain [General function prediction only];


Pssm-ID: 441325 [Multi-domain]  Cd Length: 137  Bit Score: 38.14  E-value: 4.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C        3 MPKVEnPLLISLYsHYVEQILSEtnsidDANQKLRDLGKELGQQIYlnteivektkENVTTREEVAKLIENVYK----VL 78
Cdd:COG1719   1 MAAEE-DFLVALF-RALEEELGI-----AAARVLYRAGKRIGKELA----------ERFKEEADLLEALKEFWKlsgwGI 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C       79 FDkkpkdVDMKtARGSVRITDDNCVWCqevnlEGMRGFGY--CEIFSGILESILEFK-GVDAKVFQEMSKATGSDVCVWN 155
Cdd:COG1719  64 LE-----IDEL-SEGPLVITVEDSPEC-----RGLPNSGKpvCHFLAGLLAGFFSELlGKEVEVRETECEAMGDDYCRFE 132


                ....
7YH3_C      156 VRLV 159
Cdd:COG1719 133 VRPK 136
TRAPPC5_Trs31 cd14943
Trs31 subunit of the TRAPP complex; TRS31 (also known as TRAPPC5) subunit of the trafficking ...
 14-139 4.86e-04

Trs31 subunit of the TRAPP complex; TRS31 (also known as TRAPPC5) subunit of the trafficking protein particle complex (TRAPP). TRS31 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.


Pssm-ID: 271346  Cd Length: 158  Bit Score: 38.28  E-value: 4.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C       14 LYSHYVEQILSETNSIDDANQKLRDLGKELGQQIYlntEIVeKTKENVTTRE----EVAKLI-ENVYKVLFDK------K 82
Cdd:cd14943   9 LFSEMVQYAQRRVKSISELEQRLSELGYRVGIRLL---ELL-SLREKGPKREtrilSILQFIkTTVWKYLFGKeadsleK 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
7YH3_C       83 PKDVD---MktargsvrITDDNCVWCQEVNL-EGMRGFGYCEIFSGILESILEFKGVDAKV 139
Cdd:cd14943  85 STDDDneyM--------IIDNEPLVNKFISVpKDMGGLNCAAFVAGIIEGVLDSAGFPAKV 137
 
Name Accession Description Interval E-value
TRAPP pfam04051
Transport protein particle (TRAPP) component; TRAPP plays a key role in the targeting and/or ...
 14-139 4.29e-06

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: 44.00  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C         14 LYSHYVEQILSETNSIDDANQKLRDLGKELGQQIylnteiVE----KTKENVTTRE-EVAKLI-ENVYKVLFDKKPKDVd 87
Cdd:pfam04051   4 LYGELVAYLQKDSEDVEEVNKRLEKMGYNIGQRL------IElflaRDSRCRFTDFlETLKFIcKDVWKMLFGKQADNL- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
7YH3_C         88 mKTARGSVRITDDNCVWCQE-VNL-EGMRGFGYCEIFSGILESILEFKGVDAKV 139
Cdd:pfam04051  77 -ETNHDGEYVLIDNEPPLTRfVELpKDGSQLNYLAFLCGIIRGALEMLGFPARV 129
COG1719 COG1719
Predicted hydrocarbon binding protein, contains 4VR domain [General function prediction only];
3-159 4.83e-04

Predicted hydrocarbon binding protein, contains 4VR domain [General function prediction only];


Pssm-ID: 441325 [Multi-domain]  Cd Length: 137  Bit Score: 38.14  E-value: 4.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C        3 MPKVEnPLLISLYsHYVEQILSEtnsidDANQKLRDLGKELGQQIYlnteivektkENVTTREEVAKLIENVYK----VL 78
Cdd:COG1719   1 MAAEE-DFLVALF-RALEEELGI-----AAARVLYRAGKRIGKELA----------ERFKEEADLLEALKEFWKlsgwGI 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C       79 FDkkpkdVDMKtARGSVRITDDNCVWCqevnlEGMRGFGY--CEIFSGILESILEFK-GVDAKVFQEMSKATGSDVCVWN 155
Cdd:COG1719  64 LE-----IDEL-SEGPLVITVEDSPEC-----RGLPNSGKpvCHFLAGLLAGFFSELlGKEVEVRETECEAMGDDYCRFE 132


                ....
7YH3_C      156 VRLV 159
Cdd:COG1719 133 VRPK 136
TRAPPC5_Trs31 cd14943
Trs31 subunit of the TRAPP complex; TRS31 (also known as TRAPPC5) subunit of the trafficking ...
 14-139 4.86e-04

Trs31 subunit of the TRAPP complex; TRS31 (also known as TRAPPC5) subunit of the trafficking protein particle complex (TRAPP). TRS31 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.


Pssm-ID: 271346  Cd Length: 158  Bit Score: 38.28  E-value: 4.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YH3_C       14 LYSHYVEQILSETNSIDDANQKLRDLGKELGQQIYlntEIVeKTKENVTTRE----EVAKLI-ENVYKVLFDK------K 82
Cdd:cd14943   9 LFSEMVQYAQRRVKSISELEQRLSELGYRVGIRLL---ELL-SLREKGPKREtrilSILQFIkTTVWKYLFGKeadsleK 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
7YH3_C       83 PKDVD---MktargsvrITDDNCVWCQEVNL-EGMRGFGYCEIFSGILESILEFKGVDAKV 139
Cdd:cd14943  85 STDDDneyM--------IIDNEPLVNKFISVpKDMGGLNCAAFVAGIIEGVLDSAGFPAKV 137
 
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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