N(alpha)-acetyltransferase 38, NatC auxiliary subunit [Mus musculus]
LSM domain-containing protein( domain architecture ID 10150548)
LSM domain-containing protein similar to U6 snRNA-associated Sm-like LSM domain-containing 1 (LSMD1), which is involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation, and similar to an auxillary component of the N-terminal acetyltransferase C complex, which acetylates N-terminal methionines
List of domain hits
Name | Accession | Description | Interval | E-value | ||
LSMD1 | cd06168 | LSM domain containing 1; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ... |
42-115 | 1.55e-37 | ||
LSM domain containing 1; 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. LSMD1 proteins have a single Sm-like domain structure. Sm-like proteins exist in archaea as well as prokaryotes, forming heptameric and hexameric ring structures similar to those found in eukaryotes. : Pssm-ID: 212486 Cd Length: 73 Bit Score: 121.90 E-value: 1.55e-37
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Name | Accession | Description | Interval | E-value | ||
LSMD1 | cd06168 | LSM domain containing 1; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ... |
42-115 | 1.55e-37 | ||
LSM domain containing 1; 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. LSMD1 proteins have a single Sm-like domain structure. Sm-like proteins exist in archaea as well as prokaryotes, forming heptameric and hexameric ring structures similar to those found in eukaryotes. Pssm-ID: 212486 Cd Length: 73 Bit Score: 121.90 E-value: 1.55e-37
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Sm | smart00651 | snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ... |
44-114 | 5.35e-13 | ||
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing Pssm-ID: 197820 [Multi-domain] Cd Length: 67 Bit Score: 59.05 E-value: 5.35e-13
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LSM | pfam01423 | LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ... |
45-114 | 7.49e-13 | ||
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: 58.67 E-value: 7.49e-13
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Name | Accession | Description | Interval | E-value | ||
LSMD1 | cd06168 | LSM domain containing 1; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ... |
42-115 | 1.55e-37 | ||
LSM domain containing 1; 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. LSMD1 proteins have a single Sm-like domain structure. Sm-like proteins exist in archaea as well as prokaryotes, forming heptameric and hexameric ring structures similar to those found in eukaryotes. Pssm-ID: 212486 Cd Length: 73 Bit Score: 121.90 E-value: 1.55e-37
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Sm_B | cd01717 | Sm protein B; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a ... |
45-115 | 1.14e-15 | ||
Sm protein B; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a hetero-heptameric ring around the Sm site of the 2,2,7-trimethyl guanosine (m3G) capped U1, U2, U4 and U5 snRNAs (Sm snRNAs) forming the core of the snRNP particle. The snRNP particle, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. 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. Pssm-ID: 212464 Cd Length: 80 Bit Score: 66.42 E-value: 1.14e-15
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Sm_like | cd00600 | Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ... |
45-113 | 5.35e-15 | ||
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: 64.19 E-value: 5.35e-15
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Sm | smart00651 | snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ... |
44-114 | 5.35e-13 | ||
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing Pssm-ID: 197820 [Multi-domain] Cd Length: 67 Bit Score: 59.05 E-value: 5.35e-13
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LSM | pfam01423 | LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ... |
45-114 | 7.49e-13 | ||
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: 58.67 E-value: 7.49e-13
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LSm7 | cd01729 | Like-Sm protein 7; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ... |
45-112 | 3.11e-05 | ||
Like-Sm protein 7; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm657 is believed to be an assembly intermediate for both the LSm1-7 and LSm2-8 rings. 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. Pssm-ID: 212476 Cd Length: 89 Bit Score: 39.88 E-value: 3.11e-05
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LSm8 | cd01727 | Like-Sm protein 8; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ... |
45-112 | 5.79e-04 | ||
Like-Sm protein 8; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus uridylation tag of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. LSm2-8 form the core of the snRNP particle that, in turn, assembles with other components onto the pre-mRNA to form the spliceosome which is responsible for the excision of introns and the ligation of exons. LSm1-7 is involved in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm657 is believed to be an assembly intermediate for both the LSm1-7 and LSm2-8 rings. 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. Pssm-ID: 212474 Cd Length: 91 Bit Score: 36.35 E-value: 5.79e-04
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Gemin6 | cd11676 | Gemin 6; Gemins 6, together with the survival motor neuron (SMN) protein, other Gemins, and ... |
45-115 | 2.34e-03 | ||
Gemin 6; Gemins 6, together with the survival motor neuron (SMN) protein, other Gemins, and Unr-interacting protein (UNRIP) form the SMN complex, which plays an important role in the Sm core assembly reaction, by binding directly to the Sm proteins, as well as UsnRNAs. Gemin 6 forms a heterodimer with Gemin 7, which serve as a surrogate for the SmB-SmD3 dimer during the formation of the heptameric Sm ring. Pssm-ID: 212487 Cd Length: 63 Bit Score: 34.16 E-value: 2.34e-03
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Blast search parameters | ||||
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