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Conserved domains on  [gi|74229021|ref|NP_001027903|]
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2'-5'-oligoadenylate synthase 2 isoform 3 [Homo sapiens]

Protein Classification

nucleotidyltransferase( domain architecture ID 10143781)

nucleotidyltransferase (NT), similar to the small 65-kd isoform of human 2'-5'-oligoadenylate synthase-like protein, belongs to the Pol beta-like NT superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
31-150 1.78e-17

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family.


:

Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 74.36  E-value: 1.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229021  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74229021 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALS 150
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADS 114
 
Name Accession Description Interval E-value
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
31-150 1.78e-17

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 74.36  E-value: 1.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229021  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74229021 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALS 150
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADS 114
 
Name Accession Description Interval E-value
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
31-150 1.78e-17

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 74.36  E-value: 1.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74229021  31 QTLIDEMVNTICDVLQEPEQFP--LVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDqkRSQRDILDKTGDKLKfc 108
Cdd:cd05400   2 LEEAKERYREIREALKESLSELagRVAEVFLQGSYARGTALRGDSDIDLVVVLPDDTSFAE--YGPAELLDELGEALK-- 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74229021 109 lftKWLKNNFEIQKSLDGFTIQVftKNQRISFEVLAAFNALS 150
Cdd:cd05400  78 ---EYYGANEEVKAQHRSVTVKF--KGQGFHVDVVPAFEADS 114
 
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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