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Conserved domains on  [gi|987996548|ref|NP_001306914|]
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protein mago nashi homolog 2 isoform 2 [Homo sapiens]

Protein Classification

mago nashi family protein( domain architecture ID 3306)

mago nashi family protein is an integral member of the exon junction complex (EJC), which is a multiprotein complex consisting of 4 core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14); Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity

CATH:  3.30.1560.10
Gene Ontology:  GO:0008380|GO:0035145|GO:0051028|GO:0006397|GO:0003723
SCOP:  4000574

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mago_nashi super family cl03715
Mago nashi proteins, integral members of the exon junction complex; Members of this family, ...
 1-102 3.29e-78

Mago nashi proteins, integral members of the exon junction complex; Members of this family, which was originally identified in Drosophila and called mago nashi, are integral members of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. In humans, but not Drosophila, EJC is involved in nonsense-mediated mRNA decay (NMD) via binding to Upf3b, a central NMD effector. EJC is stripped off the mRNA during the first round of translation and then the complex components are transported back into the nucleus and recycled. The Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13.


The actual alignment was detected with superfamily member cd11295:

Pssm-ID: 470860  Cd Length: 143  Bit Score: 225.99  E-value: 3.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987996548   1 MIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYY 80
Cdd:cd11295   42 MIRKEAYVSPAVLEELKRIIEDSEILKEDDAKWPEPDRVGRQELEIVMGDEHISFTTSKIGSLVDVQQSKDPEGLRVFYY 121

                         90       100
                 ....*....|....*....|..
gi 987996548  81 LVQDLKCLVFSLIGLHFKIKPI 102
Cdd:cd11295  122 LVQDLKCLVFSLIGLHFKIKPI 143
 
Name Accession Description Interval E-value
Mago_nashi cd11295
Mago nashi proteins, integral members of the exon junction complex; Members of this family, ...
 1-102 3.29e-78

Mago nashi proteins, integral members of the exon junction complex; Members of this family, which was originally identified in Drosophila and called mago nashi, are integral members of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. In humans, but not Drosophila, EJC is involved in nonsense-mediated mRNA decay (NMD) via binding to Upf3b, a central NMD effector. EJC is stripped off the mRNA during the first round of translation and then the complex components are transported back into the nucleus and recycled. The Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13.


Pssm-ID: 199917  Cd Length: 143  Bit Score: 225.99  E-value: 3.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987996548   1 MIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYY 80
Cdd:cd11295   42 MIRKEAYVSPAVLEELKRIIEDSEILKEDDAKWPEPDRVGRQELEIVMGDEHISFTTSKIGSLVDVQQSKDPEGLRVFYY 121

                         90       100
                 ....*....|....*....|..
gi 987996548  81 LVQDLKCLVFSLIGLHFKIKPI 102
Cdd:cd11295  122 LVQDLKCLVFSLIGLHFKIKPI 143
Mago_nashi pfam02792
Mago nashi protein; This family was originally identified in Drosophila and called mago nashi, ...
 1-102 2.81e-77

Mago nashi protein; This family was originally identified in Drosophila and called mago nashi, it is a strict maternal effect, grandchildless-like, gene. The human homolog has been shown to interact with an RNA binding protein. An RNAi knockout of the C. elegans homolog causes masculinization of the germ line (Mog phenotype) hermaphrodites, suggesting it is involved in hermaphrodite germ-line sex determination. Mago nashi has been found to be part of the exon-exon junction complex that binds 20 nucleotides upstream of exon-exon junctions.


Pssm-ID: 460697  Cd Length: 142  Bit Score: 223.64  E-value: 2.81e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987996548    1 MIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYY 80
Cdd:pfam02792  41 LIRKEVYVSPAVLEELKRIIEDSEILKEDDAKWPEPDRVGRQELEIVLGNEHISFTTSKIGSLSDVQNSKDPEGLRVFYY 120

                          90       100
                  ....*....|....*....|..
gi 987996548   81 LVQDLKCLVFSLIGLHFKIKPI 102
Cdd:pfam02792 121 LVQDLKCLVFSLISLHFKIKPI 142
 
Name Accession Description Interval E-value
Mago_nashi cd11295
Mago nashi proteins, integral members of the exon junction complex; Members of this family, ...
 1-102 3.29e-78

Mago nashi proteins, integral members of the exon junction complex; Members of this family, which was originally identified in Drosophila and called mago nashi, are integral members of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. In humans, but not Drosophila, EJC is involved in nonsense-mediated mRNA decay (NMD) via binding to Upf3b, a central NMD effector. EJC is stripped off the mRNA during the first round of translation and then the complex components are transported back into the nucleus and recycled. The Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13.


Pssm-ID: 199917  Cd Length: 143  Bit Score: 225.99  E-value: 3.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987996548   1 MIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYY 80
Cdd:cd11295   42 MIRKEAYVSPAVLEELKRIIEDSEILKEDDAKWPEPDRVGRQELEIVMGDEHISFTTSKIGSLVDVQQSKDPEGLRVFYY 121

                         90       100
                 ....*....|....*....|..
gi 987996548  81 LVQDLKCLVFSLIGLHFKIKPI 102
Cdd:cd11295  122 LVQDLKCLVFSLIGLHFKIKPI 143
Mago_nashi pfam02792
Mago nashi protein; This family was originally identified in Drosophila and called mago nashi, ...
 1-102 2.81e-77

Mago nashi protein; This family was originally identified in Drosophila and called mago nashi, it is a strict maternal effect, grandchildless-like, gene. The human homolog has been shown to interact with an RNA binding protein. An RNAi knockout of the C. elegans homolog causes masculinization of the germ line (Mog phenotype) hermaphrodites, suggesting it is involved in hermaphrodite germ-line sex determination. Mago nashi has been found to be part of the exon-exon junction complex that binds 20 nucleotides upstream of exon-exon junctions.


Pssm-ID: 460697  Cd Length: 142  Bit Score: 223.64  E-value: 2.81e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987996548    1 MIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYY 80
Cdd:pfam02792  41 LIRKEVYVSPAVLEELKRIIEDSEILKEDDAKWPEPDRVGRQELEIVLGNEHISFTTSKIGSLSDVQNSKDPEGLRVFYY 120

                          90       100
                  ....*....|....*....|..
gi 987996548   81 LVQDLKCLVFSLIGLHFKIKPI 102
Cdd:pfam02792 121 LVQDLKCLVFSLISLHFKIKPI 142
 
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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