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Conserved domains on  [gi|1610576451|ref|NP_001356413|]
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protein LSM12 isoform 1 [Homo sapiens]

Protein Classification

LSm12_N and AD domain-containing protein( domain architecture ID 10109624)

LSm12_N and AD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AD smart00995
Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants ...
 78-165 1.96e-36

Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins.


:

Pssm-ID: 214962  Cd Length: 90  Bit Score: 123.57  E-value: 1.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576451   78 PLASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCK--GKE 155
Cdd:smart00995   1 PPAPVNLERVKKRLRKAIEQAKRKADSKGKGVSPEGQEIFDAIAKTIPDCRWQGKNIVVLDEVTISPPYTVENVKklSGN 80

                           90
                   ....*....|
gi 1610576451  156 GSALSHVRKI 165
Cdd:smart00995  81 SKALERVQKI 90
LSm12_N cd01735
Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that ...
 7-67 6.24e-36

Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that 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 that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm12 has a novel methyltransferase domain.


:

Pssm-ID: 212482  Cd Length: 61  Bit Score: 121.31  E-value: 6.24e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576451   7 EYFSVGSQVSCRTCQEQRLQGEVVAFDYQSKMLALKCPSSSGKPNHADILLINLQYVSEVE 67
Cdd:cd01735     1 EYFSVGSQVSCKTCFGQRIQGEVVAFDHPSKMLALKCPSSSGKPNLADISIVNLDYVSDVE 61
 
Name Accession Description Interval E-value
AD smart00995
Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants ...
 78-165 1.96e-36

Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins.


Pssm-ID: 214962  Cd Length: 90  Bit Score: 123.57  E-value: 1.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576451   78 PLASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCK--GKE 155
Cdd:smart00995   1 PPAPVNLERVKKRLRKAIEQAKRKADSKGKGVSPEGQEIFDAIAKTIPDCRWQGKNIVVLDEVTISPPYTVENVKklSGN 80

                           90
                   ....*....|
gi 1610576451  156 GSALSHVRKI 165
Cdd:smart00995  81 SKALERVQKI 90
LSm12_N cd01735
Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that ...
 7-67 6.24e-36

Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that 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 that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm12 has a novel methyltransferase domain.


Pssm-ID: 212482  Cd Length: 61  Bit Score: 121.31  E-value: 6.24e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576451   7 EYFSVGSQVSCRTCQEQRLQGEVVAFDYQSKMLALKCPSSSGKPNHADILLINLQYVSEVE 67
Cdd:cd01735     1 EYFSVGSQVSCKTCFGQRIQGEVVAFDHPSKMLALKCPSSSGKPNLADISIVNLDYVSDVE 61
AD pfam09793
Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants ...
 80-165 2.03e-30

Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins. It is an anticodon-binding domain of a prolyl-tRNA synthetase, whose PDB structure is available under the identifier 1h4q.


Pssm-ID: 462905  Cd Length: 90  Bit Score: 108.06  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576451  80 ASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCKGKEGS-- 157
Cdd:pfam09793   1 PPVDLNRLQARLRKAIEEAKAKLARIGKGVSPEGQAIFDALSKTLPDVRWKGKNIVVLDEVIIAPPYKVENCKKLGSSgn 80

                          90
                  ....*....|
gi 1610576451 158 --ALSHVRKI 165
Cdd:pfam09793  81 pkALERVKKI 90
 
Name Accession Description Interval E-value
AD smart00995
Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants ...
 78-165 1.96e-36

Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins.


Pssm-ID: 214962  Cd Length: 90  Bit Score: 123.57  E-value: 1.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576451   78 PLASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCK--GKE 155
Cdd:smart00995   1 PPAPVNLERVKKRLRKAIEQAKRKADSKGKGVSPEGQEIFDAIAKTIPDCRWQGKNIVVLDEVTISPPYTVENVKklSGN 80

                           90
                   ....*....|
gi 1610576451  156 GSALSHVRKI 165
Cdd:smart00995  81 SKALERVQKI 90
LSm12_N cd01735
Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that ...
 7-67 6.24e-36

Like-Sm protein 12, N-terminal domain; LSm12 belongs to a family of Sm-like proteins that 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 that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm12 has a novel methyltransferase domain.


Pssm-ID: 212482  Cd Length: 61  Bit Score: 121.31  E-value: 6.24e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576451   7 EYFSVGSQVSCRTCQEQRLQGEVVAFDYQSKMLALKCPSSSGKPNHADILLINLQYVSEVE 67
Cdd:cd01735     1 EYFSVGSQVSCKTCFGQRIQGEVVAFDHPSKMLALKCPSSSGKPNLADISIVNLDYVSDVE 61
AD pfam09793
Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants ...
 80-165 2.03e-30

Anticodon-binding domain; This domain of approximately 100 residues is conserved from plants to humans. It is frequently found in association with Lsm domain-containing proteins. It is an anticodon-binding domain of a prolyl-tRNA synthetase, whose PDB structure is available under the identifier 1h4q.


Pssm-ID: 462905  Cd Length: 90  Bit Score: 108.06  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576451  80 ASLNVSKLASKARTEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVITPPYQVENCKGKEGS-- 157
Cdd:pfam09793   1 PPVDLNRLQARLRKAIEEAKAKLARIGKGVSPEGQAIFDALSKTLPDVRWKGKNIVVLDEVIIAPPYKVENCKKLGSSgn 80

                          90
                  ....*....|
gi 1610576451 158 --ALSHVRKI 165
Cdd:pfam09793  81 pkALERVKKI 90
Sm_like cd00600
Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ...
 8-67 4.92e-06

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: 43.01  E-value: 4.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576451   8 YFSVGSQVSCRTCQEQRLQGEVVAFDyQSKMLALKCPSS---SGKPNHADILLINLQYVSEVE 67
Cdd:cd00600     2 KDFIGKTVSVELKDGRVLTGTLVAFD-KYMNLVLDDVVEtgrDGKVRVLGLVLIRGSNIVSIR 63
 
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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