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Conserved domains on  [gi|193885331]
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Chain G, Transport protein particle 23 kDa subunit

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TRS23 COG5122
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
1-218 6.32e-57

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


:

Pssm-ID: 227451  Cd Length: 134  Bit Score: 176.63  E-value: 6.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   1 MAIETILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPkalqltqqtnientipyipYVGmssnrs 80
Cdd:COG5122    1 MAVEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIP-------------------LPG------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  81 dtrngggnnnkhtnneklgsfkgddffkepftnwnKSGLRQLCTDQFTMFIYQTLTGLKFVAISssvmpqrqptiattdk 160
Cdd:COG5122   56 -----------------------------------SSGRLVLYFRNFVMTIFQTTTGTKFVFVA---------------- 84
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193885331 161 pdrPKSTSNLAIQiadnfLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENL 218
Cdd:COG5122   85 ---EKRTVNALFQ-----LQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
 
Name Accession Description Interval E-value
TRS23 COG5122
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
1-218 6.32e-57

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


Pssm-ID: 227451  Cd Length: 134  Bit Score: 176.63  E-value: 6.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   1 MAIETILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPkalqltqqtnientipyipYVGmssnrs 80
Cdd:COG5122    1 MAVEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIP-------------------LPG------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  81 dtrngggnnnkhtnneklgsfkgddffkepftnwnKSGLRQLCTDQFTMFIYQTLTGLKFVAISssvmpqrqptiattdk 160
Cdd:COG5122   56 -----------------------------------SSGRLVLYFRNFVMTIFQTTTGTKFVFVA---------------- 84
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193885331 161 pdrPKSTSNLAIQiadnfLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENL 218
Cdd:COG5122   85 ---EKRTVNALFQ-----LQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
TRAPPC4_synbindin cd14856
Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 ...
5-214 8.84e-56

Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 (TRAPPC4), also known as synbindin or TRS23, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic.


Pssm-ID: 341446  Cd Length: 127  Bit Score: 173.47  E-value: 8.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   5 TILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPKALQltqqtnientipyipyvgmssnrsdtrn 84
Cdd:cd14856    2 SLYIINKAGGLIYQKDFSDALAKLSSNDYLRLASTFHGLHAIAAQLSPVPGS---------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  85 gggnnnkhtnneklgsfkgddffkepftnwnkSGLRQLCTDQFTMFIYQTLTGLKFVAISSsvmpqrqptiattdkpdrp 164
Cdd:cd14856   54 --------------------------------SGIELLETDTFRLHCFQTLTGIKFVLVAD------------------- 82
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193885331 165 kstsnLAIQIADNFLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKM 214
Cdd:cd14856   83 -----PKQPGLDALLRRVYELYADYVLKNPFYELEMPIRCELFDENLQKL 127
Sybindin pfam04099
Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the ...
3-218 1.21e-30

Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses.


Pssm-ID: 282019  Cd Length: 134  Bit Score: 109.71  E-value: 1.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331    3 IETILVINKSGGLIYQRNFTNDEQ-KLNSNEYLILASTLHGVFAIASQLTPkalqltqqtnientipyipyvgmssnrsd 81
Cdd:pfam04099   1 IFSLYIFNRAGGLIYYKEWNRPKKtKLTTNEYKLLAGMLHSLHSISSKISP----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   82 trngggnnnkhtnneklgsFKGddffkepftnwnKSGLRQLCTDQFTMFIYQTLTGLKFVAIsssvmpqrqptiattdkp 161
Cdd:pfam04099  52 -------------------LPG------------SSGIESLETDTFKLHCLETLTGIKFVLV------------------ 82
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193885331  162 drpksTSNLAIQIADNFLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENL 218
Cdd:pfam04099  83 -----TDPGTGINRDSLLRKYYELYSDYVLKNPFYSLGMPIRCELFDEKLDQYVRSL 134
 
Name Accession Description Interval E-value
TRS23 COG5122
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
1-218 6.32e-57

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


Pssm-ID: 227451  Cd Length: 134  Bit Score: 176.63  E-value: 6.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   1 MAIETILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPkalqltqqtnientipyipYVGmssnrs 80
Cdd:COG5122    1 MAVEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIP-------------------LPG------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  81 dtrngggnnnkhtnneklgsfkgddffkepftnwnKSGLRQLCTDQFTMFIYQTLTGLKFVAISssvmpqrqptiattdk 160
Cdd:COG5122   56 -----------------------------------SSGRLVLYFRNFVMTIFQTTTGTKFVFVA---------------- 84
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193885331 161 pdrPKSTSNLAIQiadnfLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENL 218
Cdd:COG5122   85 ---EKRTVNALFQ-----LQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
TRAPPC4_synbindin cd14856
Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 ...
5-214 8.84e-56

Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 (TRAPPC4), also known as synbindin or TRS23, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic.


Pssm-ID: 341446  Cd Length: 127  Bit Score: 173.47  E-value: 8.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   5 TILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPKALQltqqtnientipyipyvgmssnrsdtrn 84
Cdd:cd14856    2 SLYIINKAGGLIYQKDFSDALAKLSSNDYLRLASTFHGLHAIAAQLSPVPGS---------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  85 gggnnnkhtnneklgsfkgddffkepftnwnkSGLRQLCTDQFTMFIYQTLTGLKFVAISSsvmpqrqptiattdkpdrp 164
Cdd:cd14856   54 --------------------------------SGIELLETDTFRLHCFQTLTGIKFVLVAD------------------- 82
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193885331 165 kstsnLAIQIADNFLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKM 214
Cdd:cd14856   83 -----PKQPGLDALLRRVYELYADYVLKNPFYELEMPIRCELFDENLQKL 127
TRAPPC_longin-like cd14853
Longin-like domains of Trafficking protein particle complex; Longin-like domains of a ...
4-214 3.12e-35

Longin-like domains of Trafficking protein particle complex; Longin-like domains of a subfamily of core components of the trafficking protein particle complex (TRAPP), including TRAPPC2, TRAPPC4, TRAPPC1 and a TRAPPC2L, whose function is not known. TRAPP complexes are required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic.


Pssm-ID: 341443  Cd Length: 132  Bit Score: 121.44  E-value: 3.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   4 ETILVINKSGGLIYQRNFTNDEQK--LNSNEYLILASTLHGVFAIASQLTPKAlqltqqtnientipyipyvgmssnrsd 81
Cdd:cd14853    1 FYFVVVGHHGNPLYEREFTPPGQAedDNEEEYKLLAGMLHSVRSINSKLSPNV--------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  82 trngggnnnkhtnneklgsfkgddffkepftnwNKSGLRQLCTDQFTMFIYQTLTGLKFVAISSSVMpqrqptiattdkp 161
Cdd:cd14853   54 ---------------------------------EKYLKLSDKTNEYKVHAYVTATGLKFVMLTDVLM------------- 87
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193885331 162 drpkstsnlaIQIADNFLRKVYCLYSDYVMKDPSYSMEM--PIRSNLFDEKVKKM 214
Cdd:cd14853   88 ----------DRIEDVLKNFFSDLYVLYVKKNPNPFYEPnsPIRSRLFDSKVQSL 132
Sybindin pfam04099
Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the ...
3-218 1.21e-30

Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses.


Pssm-ID: 282019  Cd Length: 134  Bit Score: 109.71  E-value: 1.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331    3 IETILVINKSGGLIYQRNFTNDEQ-KLNSNEYLILASTLHGVFAIASQLTPkalqltqqtnientipyipyvgmssnrsd 81
Cdd:pfam04099   1 IFSLYIFNRAGGLIYYKEWNRPKKtKLTTNEYKLLAGMLHSLHSISSKISP----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331   82 trngggnnnkhtnneklgsFKGddffkepftnwnKSGLRQLCTDQFTMFIYQTLTGLKFVAIsssvmpqrqptiattdkp 161
Cdd:pfam04099  52 -------------------LPG------------SSGIESLETDTFKLHCLETLTGIKFVLV------------------ 82
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193885331  162 drpksTSNLAIQIADNFLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENL 218
Cdd:pfam04099  83 -----TDPGTGINRDSLLRKYYELYSDYVLKNPFYSLGMPIRCELFDEKLDQYVRSL 134
Sedlin_N pfam04628
Sedlin, N-terminal conserved region; Mutations in this protein are associated with the ...
177-217 3.94e-05

Sedlin, N-terminal conserved region; Mutations in this protein are associated with the X-linked spondyloepiphyseal dysplasia tarda syndrome (OMIM:313400). This family represents an N-terminal conserved region.


Pssm-ID: 335859  Cd Length: 129  Bit Score: 41.86  E-value: 3.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193885331  177 NFLRKVYCLYSDYVMkDPSYSMEMPIRSNLFDEKVKKMVEN 217
Cdd:pfam04628  90 QFFQEVHELYVKTLM-NPFYKPNDPIRSPAFDKKVRKLAKK 129
TRAPPC1_MUM2 cd14855
Trafficking protein particle complex subunit 1; Trafficking protein particle complex subunit 1 ...
115-211 8.54e-05

Trafficking protein particle complex subunit 1; Trafficking protein particle complex subunit 1 (TRAPPC1), also known as MUM2 and BET5, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic.


Pssm-ID: 341445  Cd Length: 132  Bit Score: 40.99  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331 115 NKSGLRQLCTDQFTMFIYQTLTGLKFVaisssvmpqrqptiATTDkPDRPKSTsnlaiqiadNFLRKVYC-LYSDYVMKD 193
Cdd:cd14855   56 DTCGFHSYTTNKYKLHYYETPTGLKFV--------------LLTD-PNVGDLR---------DVLQQIYSnIYVEYVVKN 111
                         90
                 ....*....|....*...
gi 193885331 194 PSYSMEMPIRSNLFDEKV 211
Cdd:cd14855  112 PLYPPGEPITSELFRSKL 129
TRAPPC2L cd14854
Trafficking protein particle complex subunit 2-like; Trafficking protein particle complex ...
96-215 2.24e-03

Trafficking protein particle complex subunit 2-like; Trafficking protein particle complex subunit 2-like (TRAPPC2L) is related to TRAPPC2. Its function is not known, but there are indications that it is part of the TRAPP II complex, which is required for distinct tethering events at Golgi membranes. TRAPPC2 has been identified as a general component of transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic.


Pssm-ID: 341444  Cd Length: 135  Bit Score: 36.80  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193885331  96 EKLGSFKGDDFFKEPFTnwnksGLrqLCTDQ-FTMFIYQTLTGLKFVA-ISSSVMPQRQPTIAttdkpdrpkstsnlaiq 173
Cdd:cd14854   41 EKLSASKKGGDTSDMYL-----GL--LYPTEdYKVYGYVTNTKVKFILvLEDTNTPLRDNDVR----------------- 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 193885331 174 iadNFLRKVYCLYSDYVMkDPSYSMEMPIRSNLFDEKVKKMV 215
Cdd:cd14854   97 ---TLFRRLHNAYVDAVS-NPFYPPGTPITSKKFDRRVDSLV 134
TRAPPC2_sedlin cd14825
Trafficking protein particle complex subunit 2; Trafficking protein particle complex subunit 2 ...
177-214 2.81e-03

Trafficking protein particle complex subunit 2; Trafficking protein particle complex subunit 2 (TRAPPC2), also known as Sedlin (SEDL) or TRS20, has been identified as a component of the transport protein particle (TRAPP), required for tethering endoplasmic reticulum (ER)-derived vesicles to Golgi membranes and for Golgi traffic. In humans, deletions or point mutations in the SEDL gene cause the genetic disease spondyloepiphyseal dysplasia tarda (SEDT), an X-linked skeletal disorder.


Pssm-ID: 341429  Cd Length: 135  Bit Score: 36.74  E-value: 2.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 193885331 177 NFLRKVYCLYSDYVMkDPSYSMEMPIRSNLFDEKVKKM 214
Cdd:cd14825   94 NFFQEVYELYVKILM-NPFYEPNTPIRSPAFDRRVRAL 130
 
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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