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Conserved domains on  [gi|281365402|ref|NP_001163314|]
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uncharacterized protein Dmel_CG42554 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NRBF2_MIT super family cl28842
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
 4-64 1.18e-04

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


The actual alignment was detected with superfamily member pfam17169:

Pssm-ID: 465368  Cd Length: 83  Bit Score: 39.68  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365402    4 APLNLAHFHERRSERFIRNHRYEEAIKALETSLIYMQDAQKrvaLPKSKEVldTLTLDFQR 64
Cdd:pfam17169   3 GPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMK---LTKSEQA--HLSLELQR 58
 
Name Accession Description Interval E-value
NRBF2_MIT pfam17169
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
 4-64 1.18e-04

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 465368  Cd Length: 83  Bit Score: 39.68  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365402    4 APLNLAHFHERRSERFIRNHRYEEAIKALETSLIYMQDAQKrvaLPKSKEVldTLTLDFQR 64
Cdd:pfam17169   3 GPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMK---LTKSEQA--HLSLELQR 58
 
Name Accession Description Interval E-value
NRBF2_MIT pfam17169
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
 4-64 1.18e-04

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 465368  Cd Length: 83  Bit Score: 39.68  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365402    4 APLNLAHFHERRSERFIRNHRYEEAIKALETSLIYMQDAQKrvaLPKSKEVldTLTLDFQR 64
Cdd:pfam17169   3 GPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMK---LTKSEQA--HLSLELQR 58
 
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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