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.

                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706425   3 SALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSSSQGVEQVVLGLYIVRGDNVAVIGEIDEETDSALD 82
Cdd:cd01727  2 SLLEDYLNKRVVVITTDGRVIVGTLKGFDQTTNLILSNCHERVYSSDEGVEEVPLGLYLLRGDNVAVIGEVDEELDGSID 81

                       90
               ....*....|
gi 7706425  83 LGNIRAEPLN 92
Cdd:cd01727 82 LSKIRAEPLK 91

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.

                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706425   3 SALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSSSQGVEQVVLGLYIVRGDNVAVIGEIDEETDSALD 82
Cdd:cd01727  2 SLLEDYLNKRVVVITTDGRVIVGTLKGFDQTTNLILSNCHERVYSSDEGVEEVPLGLYLLRGDNVAVIGEVDEELDGSID 81

                       90
               ....*....|
gi 7706425  83 LGNIRAEPLN 92
Cdd:cd01727 82 LSKIRAEPLK 91

snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706425      5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSssqGVEQVVLGLYIVRGDNVAVIGE 72
Cdd:smart00651  3 LKKLIGKRVLVELKNGREYRGTLKGFDQFMNLVLEDVEETVKD---GEKKRKLGLVFIRGNNIVYIIL 67

small nuclear ribonucleoprotein; Provisional

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706425    4 ALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHErvfsSSQGVEQVVLGLYIVRGDNVAVI 70
Cdd:PRK00737  8 VLNNALNSPVLVRLKGGREFRGELQGYDIHMNLVLDNAEE----IQDGEVVRKLGKVVIRGDNVVYV 70

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.

                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706425   3 SALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSSSQGVEQVVLGLYIVRGDNVAVIGEIDEETDSALD 82
Cdd:cd01727  2 SLLEDYLNKRVVVITTDGRVIVGTLKGFDQTTNLILSNCHERVYSSDEGVEEVPLGLYLLRGDNVAVIGEVDEELDGSID 81

                       90
               ....*....|
gi 7706425  83 LGNIRAEPLN 92
Cdd:cd01727 82 LSKIRAEPLK 91

snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706425      5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSssqGVEQVVLGLYIVRGDNVAVIGE 72
Cdd:smart00651  3 LKKLIGKRVLVELKNGREYRGTLKGFDQFMNLVLEDVEETVKD---GEKKRKLGLVFIRGNNIVYIIL 67

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.

                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7706425   1 MTSALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHE-RVFSSSQGV------EQVVLGLYIVRGDNV 67
Cdd:cd01717  1 KSSKMLQYINYRMRVTLQDGRQFVGTFLAFDKHMNLVLSDCEEfRKIKPKKKKkgeereEKRVLGLVLLRGENV 74

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.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7706425   5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFsssqGVEQVVLGLYIVRGDNVAVI 70
Cdd:cd00600  1 LKDFIGKTVSVELKDGRVLTGTLVAFDKYMNLVLDDVVETGR----DGKVRVLGLVLIRGSNIVSI 62

archaeal Sm protein 1; The archaeal Sm1 proteins: The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. They function to mediate RNA-RNA interactions and RNA biogenesis. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Eukaryotic Sm proteins form part of specific small nuclear ribonucleoproteins (snRNPs) that are involved in the processing of pre-mRNAs to mature mRNAs, and are a major component of the eukaryotic spliceosome. Most snRNPs consist of seven Sm proteins (B/B', D1, D2, D3, E, F and G) arranged in a ring on a uridine-rich sequence (Sm site), plus a small nuclear RNA (snRNA) (either U1, U2, U5 or U4/6). Since archaebacteria do not have any splicing apparatus, their Sm proteins may play a more general role. Archaeal LSm proteins are likely to represent the ancestral Sm domain.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706425   4 ALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVfsssQGVEQVVLGLYIVRGDNVAVI 70
Cdd:cd01731  5 VLNESLNKNVLVKLKGGKEVRGVLKGFDQHLNLVLENAEEII----EGESVRKLGTVLVRGDNVVFI 67

Sm protein G; 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. Sm subunit G binds subunits E and F to form a trimer which then assembles onto snRNA along with the D1/D2 and D3/B heterodimers forming a seven-membered ring structure.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7706425   5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVfsssQGVEQVVLGLYIVRGDNVAVI 70
Cdd:cd01719  5 LKKYMDKRLSLKLNGNRKVSGVLRGFDPFMNLVLDDAVEEV----GDGEKTPIGMVVIRGNSIIMI 66

Sm protein F; 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. Sm subunit F is capable of forming both homo- and hetero-heptamer ring structures. To form the hetero-heptamer, Sm subunit F initially binds subunits E and G to form a trimer which then assembles onto snRNA along with the D3/B and D1/D2 heterodimers.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706425   5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVfsssQGVEQVVLGLYIVRGDNVAVIGE 72
Cdd:cd01722  6 LNGLTGKPVIVKLKWGMEYKGTLVSVDSYMNLQLANTEEYI----DGKFTGNLGEVLIRCNNVLYIRE 69

Sm protein E; 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. Sm subunit E binds subunits F and G to form a trimer which then assembles onto snRNA along with the D1/D2 and D3/B heterodimers forming a seven-membered ring structure.

                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
gi 7706425  23 IVGTLKGFDQTINLILDESHErVFSSSQGVEQvvLGLYIVRGDNVAVIGE 72
Cdd:cd01718 33 IEGKIIGFDEYMNLVLDDAEE-VHLKTNTRKP--LGRILLKGDNITLIQN 79

Like-Sm protein 6; 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.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7706425   5 LENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVfsssQGVEQVVLGLYIVRGDNV 67
Cdd:cd01726  6 LKKIIGKPVVVKLKNGVEYRGVLACLDGYMNLVLEDTEEYV----DGQLVAKYGDAFIRGNNV 64