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Conserved domains on  [gi|1868518096|ref|XP_035325754|]
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uncharacterized protein HER10_EVM0011411 [Colletotrichum scovillei]

Protein Classification

double-stranded RNA binding motif domain-containing protein( domain architecture ID 10040092)

double-stranded RNA binding motif (DSRM) domain-containing protein similar to Adult diarrheal rotavirus strain J19 non-structural protein 1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 40-97 1.47e-05

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


:

Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 39.58  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868518096  40 CREANIMPPVFQLISDRRGGRTAWSSRVTVHGRTLSArfwyDGKNLNNAKEDAAEMAL 97
Cdd:cd00048     4 CQKNKWPPPEYETVEEGGPHNPRFTCTVTVNGQTFEG----EGKSKKEAKQAAAEKAL 57
 
Name Accession Description Interval E-value
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 40-97 1.47e-05

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 39.58  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868518096  40 CREANIMPPVFQLISDRRGGRTAWSSRVTVHGRTLSArfwyDGKNLNNAKEDAAEMAL 97
Cdd:cd00048     4 CQKNKWPPPEYETVEEGGPHNPRFTCTVTVNGQTFEG----EGKSKKEAKQAAAEKAL 57
 
Name Accession Description Interval E-value
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 40-97 1.47e-05

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 39.58  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868518096  40 CREANIMPPVFQLISDRRGGRTAWSSRVTVHGRTLSArfwyDGKNLNNAKEDAAEMAL 97
Cdd:cd00048     4 CQKNKWPPPEYETVEEGGPHNPRFTCTVTVNGQTFEG----EGKSKKEAKQAAAEKAL 57
 
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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