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Conserved domains on  [gi|2462506163|ref|XP_054191115|]
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conserved oligomeric Golgi complex subunit 2 isoform X1 [Homo sapiens]

Protein Classification

DUF3510 domain-containing protein( domain architecture ID 10572251)

DUF3510 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 460-586 1.97e-52

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: 175.91  E-value: 1.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506163 460 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 539
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462506163 540 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 586
Cdd:pfam12022  81 VLSSVKKTEESLRRLKKGRKRGagSLGSSVSGEGVSDDDKIRLQLFLDV 129
 
Name Accession Description Interval E-value
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 460-586 1.97e-52

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: 175.91  E-value: 1.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506163 460 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 539
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462506163 540 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 586
Cdd:pfam12022  81 VLSSVKKTEESLRRLKKGRKRGagSLGSSVSGEGVSDDDKIRLQLFLDV 129
 
Name Accession Description Interval E-value
COG2_C pfam12022
COG complex component, COG2, C-terminal; The COG complex comprises eight proteins (COG1-8) and ...
 460-586 1.97e-52

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: 175.91  E-value: 1.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506163 460 QDLSDSCFGFLKSALEVPRLYRRTNKEVPTTASSYVDSALKPLFQLQSGHKDKLKQAIIQQWLEGTLSESTHKYYETVSD 539
Cdd:pfam12022   1 SILVERCVEPLKQVRSIPRLYRMTNKPVPTKPSPYVSNILKPLKQFLEGYGKILPDEVRQEWLTDVLEEVTSRYYELVSE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462506163 540 VLNSVKKMEESLKRLKQARKTT--PANPVGPSGGMSDDDKIRLQLALDV 586
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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