U7 snRNA-associated Sm-like protein LSm11 [Homo sapiens]
U7 snRNA-associated Sm-like protein LSm11( domain architecture ID 10109683)
U7 snRNA-associated Sm-like protein LSm11 acts as a component of the U7 snRNP complex that may play a role in 3' end processing of replication-dependent histone mRNAs
List of domain hits
Name | Accession | Description | Interval | E-value | ||
LSm11_M | cd01739 | Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with ... |
159-224 | 1.03e-26 | ||
Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSm11 is an SmD2-like subunit which binds U7 snRNA along with LSm10 and five other Sm subunits to form a 7-membered ring structure. LSm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing. : Pssm-ID: 212485 Cd Length: 63 Bit Score: 100.80 E-value: 1.03e-26
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Name | Accession | Description | Interval | E-value | ||
LSm11_M | cd01739 | Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with ... |
159-224 | 1.03e-26 | ||
Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSm11 is an SmD2-like subunit which binds U7 snRNA along with LSm10 and five other Sm subunits to form a 7-membered ring structure. LSm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing. Pssm-ID: 212485 Cd Length: 63 Bit Score: 100.80 E-value: 1.03e-26
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Sm | smart00651 | snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ... |
159-222 | 9.86e-04 | ||
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing Pssm-ID: 197820 [Multi-domain] Cd Length: 67 Bit Score: 37.09 E-value: 9.86e-04
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LSM | pfam01423 | LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ... |
185-222 | 1.98e-03 | ||
LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings. Pssm-ID: 426258 Cd Length: 66 Bit Score: 36.33 E-value: 1.98e-03
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Name | Accession | Description | Interval | E-value | ||
LSm11_M | cd01739 | Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with ... |
159-224 | 1.03e-26 | ||
Like-Sm protein 11, middle domain; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. LSm11 is an SmD2-like subunit which binds U7 snRNA along with LSm10 and five other Sm subunits to form a 7-membered ring structure. LSm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing. Pssm-ID: 212485 Cd Length: 63 Bit Score: 100.80 E-value: 1.03e-26
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Sm_like | cd00600 | Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ... |
159-224 | 1.60e-08 | ||
Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm-like proteins exist in archaea as well as prokaryotes that form heptameric and hexameric ring structures similar to those found in eukaryotes. Pssm-ID: 212462 [Multi-domain] Cd Length: 63 Bit Score: 50.71 E-value: 1.60e-08
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Sm | smart00651 | snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ... |
159-222 | 9.86e-04 | ||
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing Pssm-ID: 197820 [Multi-domain] Cd Length: 67 Bit Score: 37.09 E-value: 9.86e-04
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LSM | pfam01423 | LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ... |
185-222 | 1.98e-03 | ||
LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings. Pssm-ID: 426258 Cd Length: 66 Bit Score: 36.33 E-value: 1.98e-03
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Blast search parameters | ||||
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