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Conserved domains on  [gi|2119412668|pdb|7ELH|g]
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Chain g, Lambda 1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lambda-1 super family cl17035
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 110-174 3.90e-04

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


The actual alignment was detected with superfamily member cd11674:

Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7ELH_g       110 AKDTDKSKAQVTYSDTGINNANELSRSGNVDNEGGSNQKPMSTRIAEATSaivSKHPARVGLPPT 174
Cdd:cd11674    1 AADAAQKQSSIVSSQSGENGKNDIVPSSSVDNDGGIKTQPTSDSIAAVAN---ATKPAAVISPPQ 62
 
Name Accession Description Interval E-value
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 110-174 3.90e-04

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7ELH_g       110 AKDTDKSKAQVTYSDTGINNANELSRSGNVDNEGGSNQKPMSTRIAEATSaivSKHPARVGLPPT 174
Cdd:cd11674    1 AADAAQKQSSIVSSQSGENGKNDIVPSSSVDNDGGIKTQPTSDSIAAVAN---ATKPAAVISPPQ 62
 
Name Accession Description Interval E-value
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 110-174 3.90e-04

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7ELH_g       110 AKDTDKSKAQVTYSDTGINNANELSRSGNVDNEGGSNQKPMSTRIAEATSaivSKHPARVGLPPT 174
Cdd:cd11674    1 AADAAQKQSSIVSSQSGENGKNDIVPSSSVDNDGGIKTQPTSDSIAAVAN---ATKPAAVISPPQ 62
 
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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