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Conserved domains on  [gi|186526554|ref|NP_001119304|]
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Ubiquitin system component Cue protein [Arabidopsis thaliana]

Protein Classification

CUE domain-containing protein( domain architecture ID 10198281)

CUE domain-containing protein binds ubiquitin and may promote monoubiquitination

CATH:  1.10.8.10
Gene Ontology:  GO:0043130
PubMed:  12628920|12787494
SCOP:  4003786

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
48-82 1.85e-07

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


:

Pssm-ID: 270465  Cd Length: 38  Bit Score: 45.54  E-value: 1.85e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 186526554  48 LLDHLAAIFPDMDKQILERAIEECGDDLDSAIRCL 82
Cdd:cd14279    3 KLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
48-82 1.85e-07

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 45.54  E-value: 1.85e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 186526554  48 LLDHLAAIFPDMDKQILERAIEECGDDLDSAIRCL 82
Cdd:cd14279    3 KLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
48-82 1.85e-07

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 45.54  E-value: 1.85e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 186526554  48 LLDHLAAIFPDMDKQILERAIEECGDDLDSAIRCL 82
Cdd:cd14279    3 KLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
CUE_DMA cd14370
CUE-like DMA domain found in the DM domain gene family encodes putative transcription factors ...
49-82 5.82e-03

CUE-like DMA domain found in the DM domain gene family encodes putative transcription factors DMRTA1, DMRTA2 and DMRTA3; The DM domain proteins are related to the sexual regulators doublesex from Drosophila melanogaster and MAB-3 from Caenorhabditis elegans. Thus, they have been named as doublesex- and mab-3-related transcription factors and may be involved in sexual development or in somite development. All DM domain proteins contain a DM domain which is an unusual zinc finger motif. In addition to an N-terminal DM domain, members in this family, including DMRTA1, DMRTA2 and DMRTA3, also harbor additional CUE-like DMA domain. DMRTA1 is encoded by gene DMRT1, a vertebrate equivalent of the D. melanogaster master sex regulator gene, doublesex. In D. melanogaster, doublesex controls the terminal switch of the pathway leading to sex fate choice. DMRT1 may function as regulator of sex differentiation in vertebrate. Especially, it is required for testis differentiation, but is not involved in the gonadal sex fate choice. DMRTA2, also called Doublesex- and mab-3-related transcription factor 5 (DMRT5), is encoded by gene DMRT2. In the zebrafish, DMRT2 is involved in somite development. DMRTA2 may act as an activator of cyclin-dependent kinase inhibitor 2C (cdkn2c) during spermatogenesis. It may also play significant roles in embryonic neurogenesis. DMRTA3 is encoded by tumor suppressor gene DMRT3 which serves as a novel potential target for homozygous deletion in squamous cell carcinoma of the lung.


Pssm-ID: 270553  Cd Length: 40  Bit Score: 33.30  E-value: 5.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 186526554  49 LDHLAAIFPDMDKQILERAIEECGDDLDSAIRCL 82
Cdd:cd14370    6 IELLTRLFPHQKRSVLELILQGCGGDLVQAIEQV 39
 
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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