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        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56471705  7 TKAMILPVKFIVNLAKHKQRVSIWLFENTALRIEGTLSGFDQYINLVLTDTEEVYLKTNTRRKIGTILLKGENISVISK 85
Cdd:cd01718  1 QKVMVQPINLIFRYLQNKSRVQIWLYEQTDMRIEGKIIGFDEYMNLVLDDAEEVHLKTNTRKPLGRILLKGDNITLIQN 79

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        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56471705  7 TKAMILPVKFIVNLAKHKQRVSIWLFENTALRIEGTLSGFDQYINLVLTDTEEVYLKTNTRRKIGTILLKGENISVISK 85
Cdd:cd01718  1 QKVMVQPINLIFRYLQNKSRVQIWLYEQTDMRIEGKIIGFDEYMNLVLDDAEEVHLKTNTRKPLGRILLKGDNITLIQN 79

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56471705   25 QRVSIWLFENTALRIEGTLSGFDQYINLVLTDTEEvYLKTNTRRKIGTILLKGENISVIS 84
Cdd:pfam01423  7 LGKRVLVELKNGRELRGTLKGFDQFMNLVLDDVEE-TIKDGEVRKLGLVLIRGNNIVLIS 65

Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];

                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
gi 56471705 39 IEGTLSGFDQYINLVLTDTEEVYLKTNTrRKIGTILLKGENISVIS 84
Cdd:COG1958 27 YRGKLKGYDQHMNLVLEDAEEIDDGEVV-RKLGTVVIRGDNVVFIS 71

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        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56471705  7 TKAMILPVKFIVNLAKHKQRVSIWLFENTALRIEGTLSGFDQYINLVLTDTEEVYLKTNTRRKIGTILLKGENISVISK 85
Cdd:cd01718  1 QKVMVQPINLIFRYLQNKSRVQIWLYEQTDMRIEGKIIGFDEYMNLVLDDAEEVHLKTNTRKPLGRILLKGDNITLIQN 79

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56471705   25 QRVSIWLFENTALRIEGTLSGFDQYINLVLTDTEEvYLKTNTRRKIGTILLKGENISVIS 84
Cdd:pfam01423  7 LGKRVLVELKNGRELRGTLKGFDQFMNLVLDDVEE-TIKDGEVRKLGLVLIRGNNIVLIS 65

Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];

                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
gi 56471705 39 IEGTLSGFDQYINLVLTDTEEVYLKTNTrRKIGTILLKGENISVIS 84
Cdd:COG1958 27 YRGKLKGYDQHMNLVLEDAEEIDDGEVV-RKLGTVVIRGDNVVFIS 71

Like-Sm protein 5; 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. 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 56471705 11 ILPVKFIVNLAKHKqrvsIWLFENTALRIEGTLSGFDQYINLVLTDTEEVYLKTNTRR--KIGTILLKGENISVISK 85
Cdd:cd01732  2 ILPLELIDKCIGSK----IWIIMKSDKEFVGTLLGFDDYVNMVLEDVTEYEITPEGRKitKLDQILLNGNNIAMLVP 74

small nuclear ribonucleoprotein; Provisional

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 56471705  41 GTLSGFDQYINLVLTDTEEVyLKTNTRRKIGTILLKGENISVIS 84
Cdd:PRK00737 29 GELQGYDIHMNLVLDNAEEI-QDGEVVRKLGKVVIRGDNVVYVS 71

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        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56471705 13 PVKFIVNLakHKQRVSIWLFENTALRieGTLSGFDQYINLVLTDTEEvYLKTNTRRKIGTILLKGENISVIS 84
Cdd:cd01726  2 PSKFLKKI--IGKPVVVKLKNGVEYR--GVLACLDGYMNLVLEDTEE-YVDGQLVAKYGDAFIRGNNVLYIS 68

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
               ....*....|....*....|....*....|....*....|....*....|
gi 56471705 38 RIEGTLSGFDQYINLVLTDTEEVyLKTNTRRKIGTILLKGENISVISKIE 87
Cdd:cd01719 22 KVSGVLRGFDPFMNLVLDDAVEE-VGDGEKTPIGMVVIRGNSIIMIEALD 70

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
               ....*....|....*....|....*....|....*....|....*....|..
gi 56471705 39 IEGTLSGFDQYINLVLTDTEEVYLKTN----------TRRKIGTILLKGENI 80
Cdd:cd01717 23 FVGTFLAFDKHMNLVLSDCEEFRKIKPkkkkkgeereEKRVLGLVLLRGENV 74

Like-Sm protein 3; 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. 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
               ....*....|....*....|....*....|....*....|....*....|....*...
gi 56471705 39 IEGTLSGFDQYINLVLTDTEEVY------------LKTNTRRKIGTILLKGENISVIS 84
Cdd:cd01730 24 LRGRLHAYDQHLNMILGDVEETIttveideetyeeIYKTTKRNIPMLFVRGDGVILVS 81