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Conserved domains on  [gi|1443830909|emb|SUY60846|]
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Uncharacterised protein [[Clostridium] symbiosum]

Protein Classification

GTP_EFTU_D2 domain-containing protein( domain architecture ID 10504341)

GTP_EFTU_D2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 23-90 1.97e-06

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


:

Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 44.95  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443830909  23 VEGVVEGSSISVND--YLCLNRTDGKRIKLRVESILvTPKLEVRTAEPGKAVWLVLRGRRAKQIRRGDIL 90
Cdd:pfam03144   4 ATGRVESGTLKKGDkvRILPNGTGKKKIVTRVTSLL-MFHAPLREAVAGDNAGLILAGVGLEDIRVGDTL 72
 
Name Accession Description Interval E-value
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 23-90 1.97e-06

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 44.95  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443830909  23 VEGVVEGSSISVND--YLCLNRTDGKRIKLRVESILvTPKLEVRTAEPGKAVWLVLRGRRAKQIRRGDIL 90
Cdd:pfam03144   4 ATGRVESGTLKKGDkvRILPNGTGKKKIVTRVTSLL-MFHAPLREAVAGDNAGLILAGVGLEDIRVGDTL 72
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 6-90 2.46e-04

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 39.43  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443830909   6 FRLVVHNLKKLNGFCTAVEGVVEGSSISVNDYLCLNRTDgkrIKLRVESILVTPKlEVRTAEPGKAVWLVLRGRRAKQIR 85
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG---KEVRVRSIQVHDK-PVEEAKAGDRVALNLTGVDAKELE 76


                  ....*
gi 1443830909  86 RGDIL 90
Cdd:cd03696    77 RGFVL 81
 
Name Accession Description Interval E-value
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 23-90 1.97e-06

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 44.95  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443830909  23 VEGVVEGSSISVND--YLCLNRTDGKRIKLRVESILvTPKLEVRTAEPGKAVWLVLRGRRAKQIRRGDIL 90
Cdd:pfam03144   4 ATGRVESGTLKKGDkvRILPNGTGKKKIVTRVTSLL-MFHAPLREAVAGDNAGLILAGVGLEDIRVGDTL 72
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 6-90 2.46e-04

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 39.43  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443830909   6 FRLVVHNLKKLNGFCTAVEGVVEGSSISVNDYLCLNRTDgkrIKLRVESILVTPKlEVRTAEPGKAVWLVLRGRRAKQIR 85
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG---KEVRVRSIQVHDK-PVEEAKAGDRVALNLTGVDAKELE 76


                  ....*
gi 1443830909  86 RGDIL 90
Cdd:cd03696    77 RGFVL 81
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 20-90 7.89e-03

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 35.15  E-value: 7.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443830909  20 CTAVEGVVEGSSISVNDYLCL--NRTdgkriKLRVESILVTpKLEVRTAEPGKAVWLVLRGRRAKQIRRGDIL 90
Cdd:cd04089    14 GTVVMGKVESGTIRKGQKLVLmpNKT-----KVEVTGIYID-EEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
 
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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