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Conserved domains on  [gi|145580613|ref|NP_001077394|]
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inactive 2'-5'-oligoadenylate synthase 1B [Mus musculus]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 10311207)

nucleotidyltransferase domain-containing protein, similar to African swine fever virus repair DNA polymerase X

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 159-345 2.15e-127

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


:

Pssm-ID: 463087  Cd Length: 188  Bit Score: 363.73  E-value: 2.15e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  159 KKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKL-GDPLPPQYALELLTVYAW 237
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  238 EYGSRVTKFNTAQGFRTVLELVTKYKQLRIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLA 317
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 145580613  318 GEAATWLQYPCFKYRDGSPVCSWEVPTE 345
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_Pol-beta-like super family cl11966
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ...
 30-177 1.51e-10

Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes.


The actual alignment was detected with superfamily member cd05400:

Pssm-ID: 472251 [Multi-domain]  Cd Length: 143  Bit Score: 58.95  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  30 LREVIDALCALLKDRSFRgpVRRMRASkGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLnqQGVLIKEIKKQLCEvqher 109
Cdd:cd05400    9 YREIREALKESLSELAGR--VAEVFLQ-GSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKE----- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145580613 110 rcgvKFEVHSLRSPNSRALSFKLSapdlLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLIsgRTPPG 177
Cdd:cd05400   79 ----YYGANEEVKAQHRSVTVKFK----GQGFHVDVVPAFEADSGSKYGSVPDRDGGSWVD--RNPKH 136
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 159-345 2.15e-127

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


Pssm-ID: 463087  Cd Length: 188  Bit Score: 363.73  E-value: 2.15e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  159 KKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKL-GDPLPPQYALELLTVYAW 237
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  238 EYGSRVTKFNTAQGFRTVLELVTKYKQLRIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLA 317
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 145580613  318 GEAATWLQYPCFKYRDGSPVCSWEVPTE 345
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 30-177 1.51e-10

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: 58.95  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  30 LREVIDALCALLKDRSFRgpVRRMRASkGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLnqQGVLIKEIKKQLCEvqher 109
Cdd:cd05400    9 YREIREALKESLSELAGR--VAEVFLQ-GSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKE----- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145580613 110 rcgvKFEVHSLRSPNSRALSFKLSapdlLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLIsgRTPPG 177
Cdd:cd05400   79 ----YYGANEEVKAQHRSVTVKFK----GQGFHVDVVPAFEADSGSKYGSVPDRDGGSWVD--RNPKH 136
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
 159-345 2.15e-127

2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between 320 and 344 at the extreme C-terminal end. Oligoadenylate synthetases are antiviral enzymes that counteract vial attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication. This domain is often associated with NTP_transf_2 pfam01909.


Pssm-ID: 463087  Cd Length: 188  Bit Score: 363.73  E-value: 2.15e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  159 KKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKL-GDPLPPQYALELLTVYAW 237
Cdd:pfam10421   1 SKPSPEVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  238 EYGSRVTKFNTAQGFRTVLELVTKYKQLRIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLA 317
Cdd:pfam10421  81 EQGCGKEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLA 160

                         170       180
                  ....*....|....*....|....*...
gi 145580613  318 GEAATWLQYPCFKYRDGSPVCSWEVPTE 345
Cdd:pfam10421 161 QEAAAWLSQPCFKNGDGSPVPSWDVPPA 188
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 30-177 1.51e-10

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: 58.95  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145580613  30 LREVIDALCALLKDRSFRgpVRRMRASkGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLnqQGVLIKEIKKQLCEvqher 109
Cdd:cd05400    9 YREIREALKESLSELAGR--VAEVFLQ-GSYARGTALRGDSDIDLVVVLPDDTSFAEYG--PAELLDELGEALKE----- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145580613 110 rcgvKFEVHSLRSPNSRALSFKLSapdlLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLIsgRTPPG 177
Cdd:cd05400   79 ----YYGANEEVKAQHRSVTVKFK----GQGFHVDVVPAFEADSGSKYGSVPDRDGGSWVD--RNPKH 136
 
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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