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Conserved domains on  [gi|19113462|ref|NP_596670|]
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TRAPP complex subunit Trs23 [Schizosaccharomyces pombe]

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];
1-132 1.99e-75

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


:

Pssm-ID: 227451  Cd Length: 134  Bit Score: 220.16  E-value: 1.99e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   1 MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVL 80
Cdd:COG5122   3 VEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIPLPGSSGRLVLYFRNFVMTIFQTTTGTKFVF 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113462  81 FTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH 132
Cdd:COG5122  83 VAEKRTVNALFQLQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
 
Name Accession Description Interval E-value
TRS23 COG5122
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
1-132 1.99e-75

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


Pssm-ID: 227451  Cd Length: 134  Bit Score: 220.16  E-value: 1.99e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   1 MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVL 80
Cdd:COG5122   3 VEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIPLPGSSGRLVLYFRNFVMTIFQTTTGTKFVF 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113462  81 FTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH 132
Cdd:COG5122  83 VAEKRTVNALFQLQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
TRAPPC4_synbindin cd14856
Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 ...
 2-128 1.23e-74

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: 217.77  E-value: 1.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   2 HALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVLF 81
Cdd:cd14856   1 YSLYIINKAGGLIYQKDFSDALAKLSSNDYLRLASTFHGLHAIAAQLSPVPGSSGIELLETDTFRLHCFQTLTGIKFVLV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19113462  82 TEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRY 128
Cdd:cd14856  81 ADPKQPGLDALLRRVYELYADYVLKNPFYELEMPIRCELFDENLQKL 127
Sybindin pfam04099
Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the ...
 1-132 2.94e-67

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: 199.46  E-value: 2.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462     1 MHALIIINRAGSLIFQREFGSS-PTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFV 79
Cdd:pfam04099   1 IFSLYIFNRAGGLIYYKEWNRPkKTKLTTNEYKLLAGMLHSLHSISSKISPLPGSSGIESLETDTFKLHCLETLTGIKFV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19113462    80 LFTEKKT-TNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH 132
Cdd:pfam04099  81 LVTDPGTgINRDSLLRKYYELYSDYVLKNPFYSLGMPIRCELFDEKLDQYVRSL 134
 
Name Accession Description Interval E-value
TRS23 COG5122
Transport protein particle (TRAPP) complex subunit [Intracellular trafficking and secretion];
1-132 1.99e-75

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


Pssm-ID: 227451  Cd Length: 134  Bit Score: 220.16  E-value: 1.99e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   1 MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVL 80
Cdd:COG5122   3 VEQFFIINKSGGLIFQREFGEGETELNSNEYLILASTLHGVSAILTQTIPLPGSSGRLVLYFRNFVMTIFQTTTGTKFVF 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113462  81 FTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH 132
Cdd:COG5122  83 VAEKRTVNALFQLQKIYSLYSDYVTKNPFYSPEMPIQCSLFDEHLKRMFEGH 134
TRAPPC4_synbindin cd14856
Trafficking protein particle complex subunit 4; Trafficking protein particle complex subunit 4 ...
 2-128 1.23e-74

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: 217.77  E-value: 1.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   2 HALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVLF 81
Cdd:cd14856   1 YSLYIINKAGGLIYQKDFSDALAKLSSNDYLRLASTFHGLHAIAAQLSPVPGSSGIELLETDTFRLHCFQTLTGIKFVLV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19113462  82 TEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRY 128
Cdd:cd14856  81 ADPKQPGLDALLRRVYELYADYVLKNPFYELEMPIRCELFDENLQKL 127
Sybindin pfam04099
Sybindin-like family; Sybindin is a physiological syndecan-2 ligand on dendritic spines, the ...
 1-132 2.94e-67

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: 199.46  E-value: 2.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462     1 MHALIIINRAGSLIFQREFGSS-PTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFV 79
Cdd:pfam04099   1 IFSLYIFNRAGGLIYYKEWNRPkKTKLTTNEYKLLAGMLHSLHSISSKISPLPGSSGIESLETDTFKLHCLETLTGIKFV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19113462    80 LFTEKKT-TNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH 132
Cdd:pfam04099  81 LVTDPGTgINRDSLLRKYYELYSDYVLKNPFYSLGMPIRCELFDEKLDQYVRSL 134
TRAPPC1_MUM2 cd14855
Trafficking protein particle complex subunit 1; Trafficking protein particle complex subunit 1 ...
 2-128 1.07e-24

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: 91.45  E-value: 1.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   2 HALIIINRAGSLIFQREF---GSSPTALTPNEYLVLA-GTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMK 77
Cdd:cd14855   1 YSFYIFDRHGNCIYYREWnrpKQSSNGKSEEEEQKLMfGLLFSLKSFVRKISPTDDTCGFHSYTTNKYKLHYYETPTGLK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113462  78 FVLFTEKKTTNARLQLQKFY-ELYSDYVLKNPFYTLEMPIKCQLFDEQLKRY 128
Cdd:cd14855  81 FVLLTDPNVGDLRDVLQQIYsNIYVEYVVKNPLYPPGEPITSELFRSKLDQY 132
TRAPPC_longin-like cd14853
Longin-like domains of Trafficking protein particle complex; Longin-like domains of a ...
 2-128 6.78e-24

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: 89.47  E-value: 6.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   2 HALIIINRAGSLIFQREFGSSPTALTPN--EYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFV 79
Cdd:cd14853   1 FYFVVVGHHGNPLYEREFTPPGQAEDDNeeEYKLLAGMLHSVRSINSKLSPNVEKYLKLSDKTNEYKVHAYVTATGLKFV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113462  80 LFTEKKTTNARLQLQ-KFYELYSDYVLKNPFYTLEM--PIKCQLFDEQLKRY 128
Cdd:cd14853  81 MLTDVLMDRIEDVLKnFFSDLYVLYVKKNPNPFYEPnsPIRSRLFDSKVQSL 132
Sedlin_N pfam04628
Sedlin, N-terminal conserved region; Mutations in this protein are associated with the ...
 72-131 1.60e-08

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: 49.57  E-value: 1.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113462    72 THTGMKFVLFTE---KKTTNARLQLQKFYELYSDYVLkNPFYTLEMPIKCQLFDEQLKRYIDS 131
Cdd:pfam04628  68 TNSHIKFILVHEsstKSDENIKQFFQEVHELYVKTLM-NPFYKPNDPIRSPAFDKKVRKLAKK 129
TRAPPC2_sedlin cd14825
Trafficking protein particle complex subunit 2; Trafficking protein particle complex subunit 2 ...
 1-128 4.68e-06

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: 42.90  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113462   1 MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIhgVHA----ISTQISplpGSSGIQLLEAGTFN-MHI--LQTH 73
Cdd:cd14825   1 SYYFVIVGPNDNPLYEAEFGSSKKSEFRDDHRHLNQFI--AHAaldlVDELQW---TTNNMYLKSVDRFNeWSVsaFVTA 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113462  74 TGMKFVLFTEKKTTNA-RLQLQKFYELYSdYVLKNPFYTLEMPIKCQLFDEQLKRY 128
Cdd:cd14825  76 GNIRFLLLHDNKNDDGiKNFFQEVYELYV-KILMNPFYEPNTPIRSPAFDRRVRAL 130
TRAPPC2L cd14854
Trafficking protein particle complex subunit 2-like; Trafficking protein particle complex ...
 71-127 3.34e-05

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: 40.65  E-value: 3.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113462  71 QTHTGMKFVLFTEkkTTNA-------RLQLQKFYELYSDYVLkNPFYTLEMPIKCQLFDEQLKR 127
Cdd:cd14854  72 VTNTKVKFILVLE--DTNTplrdndvRTLFRRLHNAYVDAVS-NPFYPPGTPITSKKFDRRVDS 132
TRS20 COG5603
Subunit of TRAPP, an ER-Golgi tethering complex [Cell motility and secretion];
72-126 2.32e-03

Subunit of TRAPP, an ER-Golgi tethering complex [Cell motility and secretion];


Pssm-ID: 227890  Cd Length: 136  Bit Score: 35.66  E-value: 2.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113462  72 THTGMKFVLFTEKKT-TNARLQLQKFYELYSDyVLKNPFYTLEMPIKCQLFDEQLK 126
Cdd:COG5603  75 MPSGMKFLFIHQNQSrKNARSFLQEVHELYAK-TLMSPFYEPDEPIRSQAFDDGVR 129
 
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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