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Conserved domains on  [gi|2329485236|gb|UZO15328.1|]
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hypothetical protein OCT59_006757 [Rhizophagus irregularis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eIF-3_zeta super family cl46347
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
93-144 3.80e-16

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


The actual alignment was detected with superfamily member pfam05091:

Pssm-ID: 480687  Cd Length: 521  Bit Score: 73.80  E-value: 3.80e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2329485236  93 LNLDVENVEDISLHGFLYYYDKNYDLIRTKSEKPLTPNDKVQYFDSTSKDPI 144
Cdd:pfam05091 177 LNLEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPV 228
 
Name Accession Description Interval E-value
eIF-3_zeta pfam05091
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
93-144 3.80e-16

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


Pssm-ID: 461547  Cd Length: 521  Bit Score: 73.80  E-value: 3.80e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2329485236  93 LNLDVENVEDISLHGFLYYYDKNYDLIRTKSEKPLTPNDKVQYFDSTSKDPI 144
Cdd:pfam05091 177 LNLEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPV 228
 
Name Accession Description Interval E-value
eIF-3_zeta pfam05091
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
93-144 3.80e-16

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


Pssm-ID: 461547  Cd Length: 521  Bit Score: 73.80  E-value: 3.80e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2329485236  93 LNLDVENVEDISLHGFLYYYDKNYDLIRTKSEKPLTPNDKVQYFDSTSKDPI 144
Cdd:pfam05091 177 LNLEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPV 228
 
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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