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Conserved domains on  [gi|568936773|ref|XP_006530183|]
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inactive 2'-5' oligoadenylate synthetase 1C isoform X3 [Mus musculus]

Protein Classification

OAS1_C domain-containing protein( domain architecture ID 10564343)

OAS1_C domain-containing protein

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, ...
36-218 2.12e-116

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: 329.45  E-value: 2.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773   36 KVYAQLIHECTTLEKEGDFSICFTDLHQNFMRYRAPKLWNLIRLVKHWYQLCKEKL-REPLPPQYALELLTVYVWEHSNK 114
Cdd:pfam10421   6 EVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAWEQGCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773  115 nQEKVTTAKNFRTFLELVAYYKNLRIYWTWYYDFRHQEVCAYLCRQLKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQ 194
Cdd:pfam10421  86 -KEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQEAA 164
                         170       180
                  ....*....|....*....|....
gi 568936773  195 TWMQSSCFRNCDMSFVPTWDLSPE 218
Cdd:pfam10421 165 AWLSQPCFKNGDGSPVPSWDVPPA 188
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
36-218 2.12e-116

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: 329.45  E-value: 2.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773   36 KVYAQLIHECTTLEKEGDFSICFTDLHQNFMRYRAPKLWNLIRLVKHWYQLCKEKL-REPLPPQYALELLTVYVWEHSNK 114
Cdd:pfam10421   6 EVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAWEQGCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773  115 nQEKVTTAKNFRTFLELVAYYKNLRIYWTWYYDFRHQEVCAYLCRQLKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQ 194
Cdd:pfam10421  86 -KEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQEAA 164
                         170       180
                  ....*....|....*....|....
gi 568936773  195 TWMQSSCFRNCDMSFVPTWDLSPE 218
Cdd:pfam10421 165 AWLSQPCFKNGDGSPVPSWDVPPA 188
 
Name Accession Description Interval E-value
OAS1_C pfam10421
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus; This is the largely alpha-helical, ...
36-218 2.12e-116

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: 329.45  E-value: 2.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773   36 KVYAQLIHECTTLEKEGDFSICFTDLHQNFMRYRAPKLWNLIRLVKHWYQLCKEKL-REPLPPQYALELLTVYVWEHSNK 114
Cdd:pfam10421   6 EVYVDLIRSCTSLAKPGEFSPCFTELQRNFVKSRPTKLKSLIRLVKHWYQQCKKKLkGASLPPQYALELLTVYAWEQGCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936773  115 nQEKVTTAKNFRTFLELVAYYKNLRIYWTWYYDFRHQEVCAYLCRQLKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQ 194
Cdd:pfam10421  86 -KEDFNTAEGFRTVLELIQQYQQLCIYWTVYYDFEDETVRNFLLKQLKKPRPVILDPADPTGNVGGGDRWRWDLLAQEAA 164
                         170       180
                  ....*....|....*....|....
gi 568936773  195 TWMQSSCFRNCDMSFVPTWDLSPE 218
Cdd:pfam10421 165 AWLSQPCFKNGDGSPVPSWDVPPA 188
 
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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