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Conserved domains on  [gi|1316032051|ref|NP_001346077|]
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U6 snRNA-associated Sm-like protein LSm7 isoform 3 [Mus musculus]

Protein Classification

U6 snRNA-associated Sm-like protein LSm7( domain architecture ID 10109606)

U6 snRNA-associated Sm-like protein LSm7 plays role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as a component of the precatalytic spliceosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LSm7 cd01729
Like-Sm protein 7; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 10-98 1.86e-60

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: 179.32  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  10 KESILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPDDQYKLTEDTRQLGLVVCRGTSVVLICPQD 89
Cdd:cd01729     1 KESILDLSKYVDKKIRVKFQGGREVTGILKGYDQLLNLVLDDTVEYLRDPEDPYKLTDETRSLGLVVCRGTSVVLISPVD 80


                  ....*....
gi 1316032051  90 GMEAIPNPF 98
Cdd:cd01729    81 GTEEIENPF 89
 
Name Accession Description Interval E-value
LSm7 cd01729
Like-Sm protein 7; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 10-98 1.86e-60

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: 179.32  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  10 KESILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPDDQYKLTEDTRQLGLVVCRGTSVVLICPQD 89
Cdd:cd01729     1 KESILDLSKYVDKKIRVKFQGGREVTGILKGYDQLLNLVLDDTVEYLRDPEDPYKLTDETRSLGLVVCRGTSVVLISPVD 80


                  ....*....
gi 1316032051  90 GMEAIPNPF 98
Cdd:cd01729    81 GTEEIENPF 89
LSM pfam01423
LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ...
 14-87 1.28e-20

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: 77.93  E-value: 1.28e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051  14 LDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPddqyklteDTRQLGLVVCRGTSVVLICP 87
Cdd:pfam01423   1 KFLKKLLGKRVLVELKNGRELRGTLKGFDQFMNLVLDDVEETIKDG--------EVRKLGLVLIRGNNIVLISP 66
Sm smart00651
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ...
 14-87 6.98e-20

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


Pssm-ID: 197820 [Multi-domain]  Cd Length: 67  Bit Score: 75.99  E-value: 6.98e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051   14 LDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqyklTEDTRQLGLVVCRGTSVVLICP 87
Cdd:smart00651   1 KFLKKLIGKRVLVELKNGREYRGTLKGFDQFMNLVLEDVEETVKD-------GEKKRKLGLVFIRGNNIVYIIL 67
LSM1 COG1958
Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];
16-85 1.36e-14

Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];


Pssm-ID: 441561  Cd Length: 71  Bit Score: 62.51  E-value: 1.36e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqykltEDTRQLGLVVCRGTSVVLI 85
Cdd:COG1958     9 LEKSLGKRVLVKLKDGREYRGKLKGYDQHMNLVLEDAEEIDDG--------EVVRKLGTVVIRGDNVVFI 70
PRK00737 PRK00737
small nuclear ribonucleoprotein; Provisional
 14-87 1.39e-10

small nuclear ribonucleoprotein; Provisional


Pssm-ID: 179104  Cd Length: 72  Bit Score: 52.69  E-value: 1.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316032051  14 LD-LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTmEYMRDpddqyklTEDTRQLGLVVCRGTSVVLICP 87
Cdd:PRK00737    6 LDvLNNALNSPVLVRLKGGREFRGELQGYDIHMNLVLDNA-EEIQD-------GEVVRKLGKVVIRGDNVVYVSP 72
 
Name Accession Description Interval E-value
LSm7 cd01729
Like-Sm protein 7; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 10-98 1.86e-60

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: 179.32  E-value: 1.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  10 KESILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPDDQYKLTEDTRQLGLVVCRGTSVVLICPQD 89
Cdd:cd01729     1 KESILDLSKYVDKKIRVKFQGGREVTGILKGYDQLLNLVLDDTVEYLRDPEDPYKLTDETRSLGLVVCRGTSVVLISPVD 80


                  ....*....
gi 1316032051  90 GMEAIPNPF 98
Cdd:cd01729    81 GTEEIENPF 89
LSM pfam01423
LSM domain; The LSM domain contains Sm proteins as well as other related LSM (Like Sm) ...
 14-87 1.28e-20

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: 77.93  E-value: 1.28e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051  14 LDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPddqyklteDTRQLGLVVCRGTSVVLICP 87
Cdd:pfam01423   1 KFLKKLLGKRVLVELKNGRELRGTLKGFDQFMNLVLDDVEETIKDG--------EVRKLGLVLIRGNNIVLISP 66
Sm smart00651
snRNP Sm proteins; small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA ...
 14-87 6.98e-20

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


Pssm-ID: 197820 [Multi-domain]  Cd Length: 67  Bit Score: 75.99  E-value: 6.98e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051   14 LDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqyklTEDTRQLGLVVCRGTSVVLICP 87
Cdd:smart00651   1 KFLKKLIGKRVLVELKNGREYRGTLKGFDQFMNLVLEDVEETVKD-------GEKKRKLGLVFIRGNNIVYIIL 67
Sm_G cd01719
Sm protein G; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a ...
 15-89 7.53e-19

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.


Pssm-ID: 212466  Cd Length: 70  Bit Score: 73.32  E-value: 7.53e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316032051  15 DLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqyklTEDTRqLGLVVCRGTSVVLICPQD 89
Cdd:cd01719     4 ELKKYMDKRLSLKLNGNRKVSGVLRGFDPFMNLVLDDAVEEVGD-------GEKTP-IGMVVIRGNSIIMIEALD 70
LSM1 COG1958
Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];
16-85 1.36e-14

Small nuclear ribonucleoprotein (snRNP) homolog [Transcription];


Pssm-ID: 441561  Cd Length: 71  Bit Score: 62.51  E-value: 1.36e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqykltEDTRQLGLVVCRGTSVVLI 85
Cdd:COG1958     9 LEKSLGKRVLVKLKDGREYRGKLKGYDQHMNLVLEDAEEIDDG--------EVVRKLGTVVIRGDNVVFI 70
archaeal_Sm1 cd01731
archaeal Sm protein 1; The archaeal Sm1 proteins: The Sm proteins are conserved in all three ...
 16-87 2.42e-13

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.


Pssm-ID: 212478  Cd Length: 69  Bit Score: 59.51  E-value: 2.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDpddqykltEDTRQLGLVVCRGTSVVLICP 87
Cdd:cd01731     6 LNESLNKNVLVKLKGGKEVRGVLKGFDQHLNLVLENAEEIIEG--------ESVRKLGTVLVRGDNVVFISP 69
Sm_like cd00600
Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ...
 16-86 7.67e-12

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: 55.33  E-value: 7.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPDDqykltedtRQLGLVVCRGTSVVLIC 86
Cdd:cd00600     1 LKDFIGKTVSVELKDGRVLTGTLVAFDKYMNLVLDDVVETGRDGKV--------RVLGLVLIRGSNIVSIR 63
PRK00737 PRK00737
small nuclear ribonucleoprotein; Provisional
 14-87 1.39e-10

small nuclear ribonucleoprotein; Provisional


Pssm-ID: 179104  Cd Length: 72  Bit Score: 52.69  E-value: 1.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316032051  14 LD-LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTmEYMRDpddqyklTEDTRQLGLVVCRGTSVVLICP 87
Cdd:PRK00737    6 LDvLNNALNSPVLVRLKGGREFRGELQGYDIHMNLVLDNA-EEIQD-------GEVVRKLGKVVIRGDNVVYVSP 72
LSMD1 cd06168
LSM domain containing 1; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ...
 13-76 2.01e-09

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: 49.48  E-value: 2.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051  13 ILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMRDPDdqyKLTEDTRQLGLVV 76
Cdd:cd06168     1 RLKLRKLLGRTLRVTLTDGRVLVGTFVCTDKDGNIILSNAEEYRKPSD---LGAEEPRSLGLVM 61
Sm_B cd01717
Sm protein B; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a ...
 16-83 3.58e-09

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: 49.09  E-value: 3.58e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYmRDPDDQYKLT----EDTRQLGLVVCRGTSVV 83
Cdd:cd01717     5 MLQYINYRMRVTLQDGRQFVGTFLAFDKHMNLVLSDCEEF-RKIKPKKKKKgeerEEKRVLGLVLLRGENVV 75
LSm8 cd01727
Like-Sm protein 8; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 16-89 3.68e-08

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: 46.75  E-value: 3.68e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMrdpddqYKLTEDTRQ--LGLVVCRGTSVVLICPQD 89
Cdd:cd01727     4 LEDYLNKRVVVITTDGRVIVGTLKGFDQTTNLILSNCHERV------YSSDEGVEEvpLGLYLLRGDNVAVIGEVD 73
LSm3 cd01730
Like-Sm protein 3; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 14-87 4.99e-08

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.


Pssm-ID: 212477  Cd Length: 82  Bit Score: 46.06  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316032051  14 LDLSKY-IDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYM----RDPDDQYKLTEDT-RQLGLVVCRGTSVVLICP 87
Cdd:cd01730     3 LDLIRLsLDERVYVKLRGDRELRGRLHAYDQHLNMILGDVEETIttveIDEETYEEIYKTTkRNIPMLFVRGDGVILVSP 82
archaeal_LSm cd11678
archaeal Like-Sm protein; The archaeal Sm-like (LSm): The Sm proteins are conserved in all ...
 18-87 6.52e-08

archaeal Like-Sm protein; The archaeal Sm-like (LSm): 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. 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: 212489  Cd Length: 69  Bit Score: 45.58  E-value: 6.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316032051  18 KYIDKTIRVKFQG-GREASGILKGFDPLLNLVLDGTMEYMRDpddqykltEDTRQLGLVVCRGTSVVLICP 87
Cdd:cd11678     7 SLVGSRIRVEMKGdENQLQGRLVAVDDYMNLHLTDTMECVGE--------EKVRSLGTVVLRGNNILLIQP 69
LSm1 cd01728
Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring ...
 13-86 7.47e-08

Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. Accumulation of uridylated RNAs in an lsm1 mutant suggests an involvement of the LSm1-7 complex in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm1-7, together with Pat1, are also called the decapping activator. 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: 212475  Cd Length: 74  Bit Score: 45.58  E-value: 7.47e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316032051  13 ILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYMrDPDDQYKLTEdtrqLGLVVCRGTSVVLIC 86
Cdd:cd01728     4 TASLEEELDKKILVVLRDGRKLIGILRSFDQFANLVLEDTVERI-IVGNQYGDIP----RGLFIIRGENVVLLG 72
LSm6 cd01726
Like-Sm protein 6; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 16-86 6.86e-05

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.


Pssm-ID: 212473  Cd Length: 68  Bit Score: 37.89  E-value: 6.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEYmrdpDDQykltEDTRQLGLVVCRGTSVVLIC 86
Cdd:cd01726     6 LKKIIGKPVVVKLKNGVEYRGVLACLDGYMNLVLEDTEEY----VDG----QLVAKYGDAFIRGNNVLYIS 68
archaeal_Sm_like cd11679
archaeal Sm-related protein; Archaeal Sm-related proteins: The Sm proteins are conserved in ...
 15-49 2.41e-04

archaeal Sm-related protein; Archaeal Sm-related 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.


Pssm-ID: 212490  Cd Length: 65  Bit Score: 36.09  E-value: 2.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1316032051  15 DLSKYIDKTIRVKFQGGREASGILKGFDPL-LNLVL 49
Cdd:cd11679     4 ELNSLLDKEVIVTLSNGKTYTGQLVGFDPSsLNIVL 39
Sm_F cd01722
Sm protein F; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a ...
 16-55 4.16e-04

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.


Pssm-ID: 212469  Cd Length: 69  Bit Score: 35.65  E-value: 4.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1316032051  16 LSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTMEY 55
Cdd:cd01722     6 LNGLTGKPVIVKLKWGMEYKGTLVSVDSYMNLQLANTEEY 45
PTZ00138 PTZ00138
small nuclear ribonucleoprotein; Provisional
 36-86 1.35e-03

small nuclear ribonucleoprotein; Provisional


Pssm-ID: 185472  Cd Length: 89  Bit Score: 34.70  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1316032051  36 GILKGFDPLLNLVLDGTMEYmrdpddqYKLTEDTRQLGLVVCRGTSVVLIC 86
Cdd:PTZ00138   43 GKILGFDEYMNMVLDDAEEV-------YTKKNTRKDLGRILLKGDNITLIM 86
LSm5 cd01732
Like-Sm protein 5; The eukaryotic LSm proteins (LSm2-8 or LSm1-7) assemble into a ...
 20-60 4.50e-03

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.


Pssm-ID: 212479 [Multi-domain]  Cd Length: 76  Bit Score: 33.37  E-value: 4.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1316032051  20 IDKTIRVK----FQGGREASGILKGFDPLLNLVLDGTMEYMRDPD 60
Cdd:cd01732     8 IDKCIGSKiwiiMKSDKEFVGTLLGFDDYVNMVLEDVTEYEITPE 52
Sm_E cd01718
Sm protein E; The eukaryotic Sm proteins (B/B', D1, D2, D3, E, F and G) assemble into a ...
 36-87 5.23e-03

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.


Pssm-ID: 212465  Cd Length: 79  Bit Score: 32.91  E-value: 5.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1316032051  36 GILKGFDPLLNLVLDGTMEYmrdpddqYKLTEDTRQLGLVVCRGTSVVLICP 87
Cdd:cd01718    35 GKIIGFDEYMNLVLDDAEEV-------HLKTNTRKPLGRILLKGDNITLIQN 79
 
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.
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