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Conserved domains on  [gi|6678676|ref|NP_031383|]
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conserved oligomeric Golgi complex subunit 2 isoform 1 [Homo sapiens]

Protein Classification

COG2 and DUF3510 domain-containing protein( domain architecture ID 10533028)

COG2 and DUF3510 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 15-147 4.18e-52

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: 177.08  E-value: 4.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676     15 LCFDKDEFMKEDFDVDHFVSDCRKRVQLEELRDDLELYYKLLKTAMVELINKDYADFVNLSTNLVGMDKALNQLSVPLGQ 94
Cdd:pfam06148   1 LCFDKHEFLAPDFDPDAFVSELRHHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6678676     95 LREEVLSLRSSVSEGIRAVDERMSKQEDIRKKKMCVLRLIQVIRSVEKIEKIL 147
Cdd:pfam06148  81 LRKEVESVRDELEARLEEVEQKLEERKALREKRESLKLLLDYDHVLEKLEKLL 133
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 573-699 1.23e-51

COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and plays critical roles in Golgi structure and function. It is necessary for retrograde trafficking in the Golgi apparatus and for protein glycosylation. This uncharacterized domain is found in the C-terminal of COG complex subunit 2 proteins. In Arabidopsis, COG2 forms a complex with FPP3/VETH1 and FPP2/VETH2 and ensures the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition.


:

Pssm-ID: 463434  Cd Length: 129  Bit Score: 175.52  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676    573 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 652
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6678676    653 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 699
Cdd:pfam12022  81 VLSSVKKTEESLRRLKKGRKRGagSLGSSVSGEGVSDDDKIRLQLFLDV 129
 
Name Accession Description Interval E-value
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 15-147 4.18e-52

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: 177.08  E-value: 4.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676     15 LCFDKDEFMKEDFDVDHFVSDCRKRVQLEELRDDLELYYKLLKTAMVELINKDYADFVNLSTNLVGMDKALNQLSVPLGQ 94
Cdd:pfam06148   1 LCFDKHEFLAPDFDPDAFVSELRHHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6678676     95 LREEVLSLRSSVSEGIRAVDERMSKQEDIRKKKMCVLRLIQVIRSVEKIEKIL 147
Cdd:pfam06148  81 LRKEVESVRDELEARLEEVEQKLEERKALREKRESLKLLLDYDHVLEKLEKLL 133
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 573-699 1.23e-51

COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and plays critical roles in Golgi structure and function. It is necessary for retrograde trafficking in the Golgi apparatus and for protein glycosylation. This uncharacterized domain is found in the C-terminal of COG complex subunit 2 proteins. In Arabidopsis, COG2 forms a complex with FPP3/VETH1 and FPP2/VETH2 and ensures the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition.


Pssm-ID: 463434  Cd Length: 129  Bit Score: 175.52  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676    573 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 652
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6678676    653 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 699
Cdd:pfam12022  81 VLSSVKKTEESLRRLKKGRKRGagSLGSSVSGEGVSDDDKIRLQLFLDV 129
 
Name Accession Description Interval E-value
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
 15-147 4.18e-52

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: 177.08  E-value: 4.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676     15 LCFDKDEFMKEDFDVDHFVSDCRKRVQLEELRDDLELYYKLLKTAMVELINKDYADFVNLSTNLVGMDKALNQLSVPLGQ 94
Cdd:pfam06148   1 LCFDKHEFLAPDFDPDAFVSELRHHVPLESLRRDLRAYLKLLRRELLELVNEDYADFVSLSTNLVGLDEKLNEVEVPLLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6678676     95 LREEVLSLRSSVSEGIRAVDERMSKQEDIRKKKMCVLRLIQVIRSVEKIEKIL 147
Cdd:pfam06148  81 LRKEVESVRDELEARLEEVEQKLEERKALREKRESLKLLLDYDHVLEKLEKLL 133
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 573-699 1.23e-51

COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and plays critical roles in Golgi structure and function. It is necessary for retrograde trafficking in the Golgi apparatus and for protein glycosylation. This uncharacterized domain is found in the C-terminal of COG complex subunit 2 proteins. In Arabidopsis, COG2 forms a complex with FPP3/VETH1 and FPP2/VETH2 and ensures the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition.


Pssm-ID: 463434  Cd Length: 129  Bit Score: 175.52  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678676    573 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 652
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6678676    653 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 699
Cdd:pfam12022  81 VLSSVKKTEESLRRLKKGRKRGagSLGSSVSGEGVSDDDKIRLQLFLDV 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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