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Conserved domains on  [gi|470437736|ref|XP_004339016|]
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uncharacterized protein ACA1_002450, partial [Acanthamoeba castellanii str. Neff]

Protein Classification

S1 domain-containing protein( domain architecture ID 10472825)

S1 domain-containing protein may bind RNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-5a pfam01287
Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be ...
 110-160 1.96e-10

Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be an initiation factor, has been shown to be required for peptide chain elongation in yeast.


:

Pssm-ID: 396035  Cd Length: 69  Bit Score: 54.12  E-value: 1.96e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 470437736  110 YQLLDMGDDGEVTLVDDDGEIKEGVTLPRPAWASAATQAFANGGDVNVLVL 160
Cdd:pfam01287   7 YQLIDISDDGFLSLMDDDGETKEDVKLPEGELGKEIKAKFEEGKDVLVTVL 57
 
Name Accession Description Interval E-value
eIF-5a pfam01287
Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be ...
 110-160 1.96e-10

Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be an initiation factor, has been shown to be required for peptide chain elongation in yeast.


Pssm-ID: 396035  Cd Length: 69  Bit Score: 54.12  E-value: 1.96e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 470437736  110 YQLLDMGDDGEVTLVDDDGEIKEGVTLPRPAWASAATQAFANGGDVNVLVL 160
Cdd:pfam01287   7 YQLIDISDDGFLSLMDDDGETKEDVKLPEGELGKEIKAKFEEGKDVLVTVL 57
S1_eIF5A cd04468
S1_eIF5A: Eukaryotic translation Initiation Factor 5A (eIF5A), S1-like RNA-binding domain. ...
 110-161 1.87e-08

S1_eIF5A: Eukaryotic translation Initiation Factor 5A (eIF5A), S1-like RNA-binding domain. eIF5A is an evolutionarily conserved protein found in eukaryotes. eIF5A is the only protein known to have the unusual amino acid hypusine. Hypusine is essential for eIF5A function and is a post-translationally modified lysine. eIF5A interacts with components of the 80S ribosome and translation elongation factors 2 (eEF2) in a hypusine-dependent manner. This C-terminal S1 domain resembles the oligonucleotides-binding fold (OB fold) which binds RNA. Moreover, eIF5A prefers binding to the actively translating ribosome. This evidence suggests that eIF5A plays a role in translation elongation instead of translation initiation as previously proposed.


Pssm-ID: 239914  Cd Length: 69  Bit Score: 48.69  E-value: 1.87e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 470437736 110 YQLLDMgDDGEVTLVDDDGEIKEGVTLPRPAWASAATQAFANGGDVNVLVLA 161
Cdd:cd04468    6 YQLIDI-DDGFLSLMDDDGETREDLKLPEGELGKEIREKFDEGKDVLVTVLS 56
PLN03107 PLN03107
eukaryotic translation initiation factor 5A; Provisional
 102-164 4.47e-08

eukaryotic translation initiation factor 5A; Provisional


Pssm-ID: 215580  Cd Length: 159  Bit Score: 50.09  E-value: 4.47e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470437736 102 CDQ--LTLVRYQLLDMGDDGEVTLVDDDGEIKEGVTLPRPAWASAA--TQAFANGGDVNVLVLAPSG 164
Cdd:PLN03107  80 CDVphVNRTDYQLIDISEDGFVSLMDESGNTKDDLKLPTEDDTLAEqiKDGFDEGKDLVVTVMSAMG 146
 
Name Accession Description Interval E-value
eIF-5a pfam01287
Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be ...
 110-160 1.96e-10

Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold; eIF5A, previously thought to be an initiation factor, has been shown to be required for peptide chain elongation in yeast.


Pssm-ID: 396035  Cd Length: 69  Bit Score: 54.12  E-value: 1.96e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 470437736  110 YQLLDMGDDGEVTLVDDDGEIKEGVTLPRPAWASAATQAFANGGDVNVLVL 160
Cdd:pfam01287   7 YQLIDISDDGFLSLMDDDGETKEDVKLPEGELGKEIKAKFEEGKDVLVTVL 57
S1_eIF5A cd04468
S1_eIF5A: Eukaryotic translation Initiation Factor 5A (eIF5A), S1-like RNA-binding domain. ...
 110-161 1.87e-08

S1_eIF5A: Eukaryotic translation Initiation Factor 5A (eIF5A), S1-like RNA-binding domain. eIF5A is an evolutionarily conserved protein found in eukaryotes. eIF5A is the only protein known to have the unusual amino acid hypusine. Hypusine is essential for eIF5A function and is a post-translationally modified lysine. eIF5A interacts with components of the 80S ribosome and translation elongation factors 2 (eEF2) in a hypusine-dependent manner. This C-terminal S1 domain resembles the oligonucleotides-binding fold (OB fold) which binds RNA. Moreover, eIF5A prefers binding to the actively translating ribosome. This evidence suggests that eIF5A plays a role in translation elongation instead of translation initiation as previously proposed.


Pssm-ID: 239914  Cd Length: 69  Bit Score: 48.69  E-value: 1.87e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 470437736 110 YQLLDMgDDGEVTLVDDDGEIKEGVTLPRPAWASAATQAFANGGDVNVLVLA 161
Cdd:cd04468    6 YQLIDI-DDGFLSLMDDDGETREDLKLPEGELGKEIREKFDEGKDVLVTVLS 56
PLN03107 PLN03107
eukaryotic translation initiation factor 5A; Provisional
 102-164 4.47e-08

eukaryotic translation initiation factor 5A; Provisional


Pssm-ID: 215580  Cd Length: 159  Bit Score: 50.09  E-value: 4.47e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470437736 102 CDQ--LTLVRYQLLDMGDDGEVTLVDDDGEIKEGVTLPRPAWASAA--TQAFANGGDVNVLVLAPSG 164
Cdd:PLN03107  80 CDVphVNRTDYQLIDISEDGFVSLMDESGNTKDDLKLPTEDDTLAEqiKDGFDEGKDLVVTVMSAMG 146
 
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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