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Conserved domains on  [gi|19112128|ref|NP_595336|]
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COG complex subunit Cog2 [Schizosaccharomyces pombe]

Protein Classification

Dor-1 like family protein( domain architecture ID 139767)

Dor-1 like family protein similar to Schizosaccharomyces pombe exocyst complex component sec5 and conserved oligomeric Golgi complex subunit 2, as well as N-terminal region of Homo sapiens syndetin (also known as EARP/GARPII complex subunit VPS50)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2 super family cl19297
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 33-145 1.69e-09

COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight proteins COG1-8. The COG complex plays critical roles in Golgi structure and function. The proposed function of the complex is to mediate the initial physical contact between transport vesicles and their membrane targets. A comparable role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex that mediates trafficking to the plasma membrane. COG2 structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. These bundles inCOG2 may act as platforms for interaction with other trafficing proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.


The actual alignment was detected with superfamily member pfam06148:

Pssm-ID: 473160  Cd Length: 133  Bit Score: 53.43  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112128    33 FSPDEFLVSKR-FLGLDGLVNELSRLFEQVNNELMLLVKDNYQDFVHLGSRMKSGNTKVSTLISSIHRSEEQLKNSKQSL 111
Cdd:pfam06148  13 FDPDAFVSELRhHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLALRKEVESVRDEL 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 19112128   112 IGHSTEIQNNLKHKQDVENEKLIASNLLLLDQIL 145
Cdd:pfam06148  93 EARLEEVEQKLEERKALREKRESLKLLLDYDHVL 126
 
Name Accession Description Interval E-value
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 33-145 1.69e-09

COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight proteins COG1-8. The COG complex plays critical roles in Golgi structure and function. The proposed function of the complex is to mediate the initial physical contact between transport vesicles and their membrane targets. A comparable role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex that mediates trafficking to the plasma membrane. COG2 structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. These bundles inCOG2 may act as platforms for interaction with other trafficing proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.


Pssm-ID: 399271  Cd Length: 133  Bit Score: 53.43  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112128    33 FSPDEFLVSKR-FLGLDGLVNELSRLFEQVNNELMLLVKDNYQDFVHLGSRMKSGNTKVSTLISSIHRSEEQLKNSKQSL 111
Cdd:pfam06148  13 FDPDAFVSELRhHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLALRKEVESVRDEL 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 19112128   112 IGHSTEIQNNLKHKQDVENEKLIASNLLLLDQIL 145
Cdd:pfam06148  93 EARLEEVEQKLEERKALREKRESLKLLLDYDHVL 126
 
Name Accession Description Interval E-value
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 33-145 1.69e-09

COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight proteins COG1-8. The COG complex plays critical roles in Golgi structure and function. The proposed function of the complex is to mediate the initial physical contact between transport vesicles and their membrane targets. A comparable role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex that mediates trafficking to the plasma membrane. COG2 structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. These bundles inCOG2 may act as platforms for interaction with other trafficing proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.


Pssm-ID: 399271  Cd Length: 133  Bit Score: 53.43  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112128    33 FSPDEFLVSKR-FLGLDGLVNELSRLFEQVNNELMLLVKDNYQDFVHLGSRMKSGNTKVSTLISSIHRSEEQLKNSKQSL 111
Cdd:pfam06148  13 FDPDAFVSELRhHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLALRKEVESVRDEL 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 19112128   112 IGHSTEIQNNLKHKQDVENEKLIASNLLLLDQIL 145
Cdd:pfam06148  93 EARLEEVEQKLEERKALREKRESLKLLLDYDHVL 126
 
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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