NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24656811|ref|NP_647811|]
View 

YTH domain containing 1, isoform A [Drosophila melanogaster]

Protein Classification

YTH domain-containing protein( domain architecture ID 15340179)

YTH domain-containing protein similar to Homo sapiens YTH domain-containing protein 1, a regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs

CATH:  3.10.590.10
PubMed:  12368078|19191354
SCOP:  4002214

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
255-391 1.08e-60

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


:

Pssm-ID: 410979  Cd Length: 133  Bit Score: 199.72  E-value: 1.08e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656811 255 RFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVawvlPPSIS 334
Cdd:cd21134   1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSPS----WPWWS 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24656811 335 PKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLF 391
Cdd:cd21134  77 QDKLGGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
 
Name Accession Description Interval E-value
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
255-391 1.08e-60

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


Pssm-ID: 410979  Cd Length: 133  Bit Score: 199.72  E-value: 1.08e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656811 255 RFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVawvlPPSIS 334
Cdd:cd21134   1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSPS----WPWWS 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24656811 335 PKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLF 391
Cdd:cd21134  77 QDKLGGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
YTH pfam04146
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ...
254-391 3.75e-58

YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.


Pssm-ID: 461195  Cd Length: 135  Bit Score: 193.10  E-value: 3.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656811   254 TRFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVAWVLppsi 333
Cdd:pfam04146   1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFIFWEA---- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24656811   334 SPKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLF 391
Cdd:pfam04146  77 DSDKWGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLF 134
 
Name Accession Description Interval E-value
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
255-391 1.08e-60

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


Pssm-ID: 410979  Cd Length: 133  Bit Score: 199.72  E-value: 1.08e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656811 255 RFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVawvlPPSIS 334
Cdd:cd21134   1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSPS----WPWWS 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24656811 335 PKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLF 391
Cdd:cd21134  77 QDKLGGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
YTH pfam04146
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ...
254-391 3.75e-58

YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.


Pssm-ID: 461195  Cd Length: 135  Bit Score: 193.10  E-value: 3.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656811   254 TRFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVAWVLppsi 333
Cdd:pfam04146   1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFIFWEA---- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24656811   334 SPKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLF 391
Cdd:pfam04146  77 DSDKWGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLF 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH