NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568926620|ref|XP_006537948|]
View 

focadhesin isoform X7 [Mus musculus]

Protein Classification

RST1 family protein( domain architecture ID 10576052)

RST1 family protein is a DUF3730 domain-containing protein similar to Arabidopsis thaliana protein RST1, which is required for the synthesis of alkanes from wax precursors and may play a role in acyl-CoA reduction to aldehydes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUF3730 pfam12530
Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals ...
 528-752 3.73e-81

Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals and RST1 (RESURRECTION 1) from plants. Focadhesin (FOCAD) is a focal adhesion protein with potential tumour suppressor function in gliomas. RST1 was originally identified in a genetic screen for factors involved in the biosynthesis of epicuticular waxes. Later, RST1 and RST1 INTERACTING PROTEIN (RIPR) have been shown to act as cofactors of the cytoplasmic exosome and the Ski complex in plants. It is involved in the suppression of siRNA-mediated silencing of transgenes and certain endogenous transcripts. Structure predictions suggest that this is an alpha-helical domain with and armadillo-like fold.


:

Pssm-ID: 463619  Cd Length: 227  Bit Score: 264.91  E-value: 3.73e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   528 IPVLMFKLGRPLDPVSYNHILYTLPTLGVHKVCVGQILRVIQLLGT---TPRLRAVTLRLLTSLWEKQDRVYPELQRFMA 604
Cdd:pfam12530    1 LPELLYALEKSSNPELVLLLLKGLPSLARHKVCVPLVLPFIQPLSSrdaSPLLQAVALRLLCKLWKGMDRVYPFLQPFLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   605 VSDaPSLSVGKELQWEKLIAKAASIRDICKQRPYQHGADMLAAISQVLNECTKPDQaTPAALVLQGLHALCQAEVVCIRS 684
Cdd:pfam12530   81 FSK-SSSSAFARSLIESLASLAASLRDICKHRPDQHGEDLVDAYSACLNECESEVP-EVQALGLELLDALCEAEVVDFSS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926620   685 TWNALSPKLSCDMRPLILKTLSELFSLVPSLTVNTVEYENFKVQVLSFLWTHTQNKN-PTVASAAYKSL 752
Cdd:pfam12530  159 AWDVIQKKLGLDYRPLVLKSLCSLFALLPQLEVDHEQYEELKLDIILILWKLENSNDdARVASAAFEAL 227
 
Name Accession Description Interval E-value
DUF3730 pfam12530
Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals ...
 528-752 3.73e-81

Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals and RST1 (RESURRECTION 1) from plants. Focadhesin (FOCAD) is a focal adhesion protein with potential tumour suppressor function in gliomas. RST1 was originally identified in a genetic screen for factors involved in the biosynthesis of epicuticular waxes. Later, RST1 and RST1 INTERACTING PROTEIN (RIPR) have been shown to act as cofactors of the cytoplasmic exosome and the Ski complex in plants. It is involved in the suppression of siRNA-mediated silencing of transgenes and certain endogenous transcripts. Structure predictions suggest that this is an alpha-helical domain with and armadillo-like fold.


Pssm-ID: 463619  Cd Length: 227  Bit Score: 264.91  E-value: 3.73e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   528 IPVLMFKLGRPLDPVSYNHILYTLPTLGVHKVCVGQILRVIQLLGT---TPRLRAVTLRLLTSLWEKQDRVYPELQRFMA 604
Cdd:pfam12530    1 LPELLYALEKSSNPELVLLLLKGLPSLARHKVCVPLVLPFIQPLSSrdaSPLLQAVALRLLCKLWKGMDRVYPFLQPFLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   605 VSDaPSLSVGKELQWEKLIAKAASIRDICKQRPYQHGADMLAAISQVLNECTKPDQaTPAALVLQGLHALCQAEVVCIRS 684
Cdd:pfam12530   81 FSK-SSSSAFARSLIESLASLAASLRDICKHRPDQHGEDLVDAYSACLNECESEVP-EVQALGLELLDALCEAEVVDFSS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926620   685 TWNALSPKLSCDMRPLILKTLSELFSLVPSLTVNTVEYENFKVQVLSFLWTHTQNKN-PTVASAAYKSL 752
Cdd:pfam12530  159 AWDVIQKKLGLDYRPLVLKSLCSLFALLPQLEVDHEQYEELKLDIILILWKLENSNDdARVASAAFEAL 227
 
Name Accession Description Interval E-value
DUF3730 pfam12530
Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals ...
 528-752 3.73e-81

Focadhesin/RST1, DUF3730; This domain of unknown function is found in Focadhesin from animals and RST1 (RESURRECTION 1) from plants. Focadhesin (FOCAD) is a focal adhesion protein with potential tumour suppressor function in gliomas. RST1 was originally identified in a genetic screen for factors involved in the biosynthesis of epicuticular waxes. Later, RST1 and RST1 INTERACTING PROTEIN (RIPR) have been shown to act as cofactors of the cytoplasmic exosome and the Ski complex in plants. It is involved in the suppression of siRNA-mediated silencing of transgenes and certain endogenous transcripts. Structure predictions suggest that this is an alpha-helical domain with and armadillo-like fold.


Pssm-ID: 463619  Cd Length: 227  Bit Score: 264.91  E-value: 3.73e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   528 IPVLMFKLGRPLDPVSYNHILYTLPTLGVHKVCVGQILRVIQLLGT---TPRLRAVTLRLLTSLWEKQDRVYPELQRFMA 604
Cdd:pfam12530    1 LPELLYALEKSSNPELVLLLLKGLPSLARHKVCVPLVLPFIQPLSSrdaSPLLQAVALRLLCKLWKGMDRVYPFLQPFLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926620   605 VSDaPSLSVGKELQWEKLIAKAASIRDICKQRPYQHGADMLAAISQVLNECTKPDQaTPAALVLQGLHALCQAEVVCIRS 684
Cdd:pfam12530   81 FSK-SSSSAFARSLIESLASLAASLRDICKHRPDQHGEDLVDAYSACLNECESEVP-EVQALGLELLDALCEAEVVDFSS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926620   685 TWNALSPKLSCDMRPLILKTLSELFSLVPSLTVNTVEYENFKVQVLSFLWTHTQNKN-PTVASAAYKSL 752
Cdd:pfam12530  159 AWDVIQKKLGLDYRPLVLKSLCSLFALLPQLEVDHEQYEELKLDIILILWKLENSNDdARVASAAFEAL 227
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH