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Conserved domains on  [gi|334302897|sp|Q9XRX5|]
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RecName: Full=Putative uncharacterized protein ANKRD13C-DT; AltName: Full=ANKRD13C divergent transcript; AltName: Full=HERV-H LTR-associating protein 3; AltName: Full=Human endogenous retrovirus-H long terminal repeat-associating protein 3

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RME-8_N super family cl44850
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-51 5.51e-03

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


The actual alignment was detected with superfamily member pfam19432:

Pssm-ID: 466078  Cd Length: 819  Bit Score: 34.90  E-value: 5.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 334302897   24 MTPRHAGCDVTEMQ----RILSQPTFTEHLLR 51
Cdd:pfam19432 474 MQPMHDNYDLRQEQlnksSLLSSKKFLEHLLD 505
 
Name Accession Description Interval E-value
RME-8_N pfam19432
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-51 5.51e-03

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


Pssm-ID: 466078  Cd Length: 819  Bit Score: 34.90  E-value: 5.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 334302897   24 MTPRHAGCDVTEMQ----RILSQPTFTEHLLR 51
Cdd:pfam19432 474 MQPMHDNYDLRQEQlnksSLLSSKKFLEHLLD 505
 
Name Accession Description Interval E-value
RME-8_N pfam19432
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-51 5.51e-03

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


Pssm-ID: 466078  Cd Length: 819  Bit Score: 34.90  E-value: 5.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 334302897   24 MTPRHAGCDVTEMQ----RILSQPTFTEHLLR 51
Cdd:pfam19432 474 MQPMHDNYDLRQEQlnksSLLSSKKFLEHLLD 505
 
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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