Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
E [auth G]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyMetallo-hydrolase/oxidoreductase8034424 3001057 SCOP2B (2022-06-29)
ASCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
JSCOP2B SuperfamilyARM repeat-like8093027 3000116 SCOP2B (2022-06-29)
BSCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
C [auth F]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
D [auth E]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
E [auth G]PF01423e6v4xG1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
HPF00753,PF11718e6v4xH2 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: PF00753,PF11718ECOD (1.6)
HPF10996e6v4xH1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF10996ECOD (1.6)
APF01423e6v4xA1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
JPF11935e6v4xJ1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF11935ECOD (1.6)
BPF01423e6v4xB1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
C [auth F]PF01423e6v4xF1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
D [auth E]PF01423e6v4xE1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
F [auth C]PF01423e6v4xC1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
G [auth D]PF01423e6v4xD1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
IPF07521,PF16661e6v4xI2 A: a+b four layersX: Metallo-hydrolase/oxidoreductase (From Topology)H: Metallo-hydrolase/oxidoreductase (From Topology)T: Metallo-hydrolase/oxidoreductaseF: PF07521,PF16661ECOD (1.6)
IPF10996e6v4xI1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF10996ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
E [auth G]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (utative)
A2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (utative)
J1.25.10.10 Mainly Alpha Alpha Horseshoe Leucine-rich Repeat Variant Leucine-rich Repeat VariantCATH (utative)
C [auth F]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (utative)
D [auth E]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (utative)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
E [auth G]PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
PF07521Zn-dependent metallo-hydrolase RNA specificity domain (RMMBL)Zn-dependent metallo-hydrolase RNA specificity domain- Motif
PF16661Metallo-beta-lactamase superfamily domain (Lactamase_B_6)Metallo-beta-lactamase superfamily domainThis family is part of the metallo-beta-lactamase superfamily.Domain
PF11718Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term (CPSF73-100_C)Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-termThis is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.Domain
PF10996Beta-Casp domain (Beta-Casp)Beta-Casp domainThe beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains [1].Domain
PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
PF11935Symplekin/PTA1 N-terminal (SYMPK_PTA1_N)Symplekin/PTA1 N-terminal- Repeat
PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
C [auth F]PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
D [auth E]PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
F [auth C]PF01423LSM domain (LSM)LSM domainThe 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) i ...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 [3]. 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.
Domain
PF07521Zn-dependent metallo-hydrolase RNA specificity domain (RMMBL)Zn-dependent metallo-hydrolase RNA specificity domain- Motif
PF16661Metallo-beta-lactamase superfamily domain (Lactamase_B_6)Metallo-beta-lactamase superfamily domainThis family is part of the metallo-beta-lactamase superfamily.Domain
PF13299Cleavage and polyadenylation factor 2 C-terminal (CPSF100_C)Cleavage and polyadenylation factor 2 C-terminal- Family
PF10996Beta-Casp domain (Beta-Casp)Beta-Casp domainThe beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains [1].Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
E [auth G]Small nuclear ribonucleoprotein G
Cleavage and polyadenylation specificity factor subunit 3
K [auth Z]U7 snRNA---
Small nuclear ribonucleoprotein Sm D3
Symplekin-
L [auth Y]modified H2a pre-mRNA---
Small nuclear ribonucleoprotein-associated proteins B and B'
C [auth F]Small nuclear ribonucleoprotein F
D [auth E]Small nuclear ribonucleoprotein E
F [auth C]U7 snRNA-associated Sm-like protein LSm10
G [auth D]U7 snRNA-associated Sm-like protein LSm11
Cleavage and polyadenylation specificity factor subunit 2

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
E [auth G]IPR044641Sm-like protein Lsm7/SmGFamily
E [auth G]IPR034098Small nuclear ribonucleoprotein GFamily
E [auth G]IPR001163Sm domain, eukaryotic/archaea-typeDomain
E [auth G]IPR047575Sm domainDomain
E [auth G]IPR010920LSM domain superfamilyHomologous Superfamily
IPR001279Metallo-beta-lactamaseDomain
IPR022712Beta-Casp domainDomain
IPR021718Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-termDomain
IPR011108Zn-dependent metallo-hydrolase, RNA specificity domainDomain
IPR036866Ribonuclease Z/Hydroxyacylglutathione hydrolase-likeHomologous Superfamily
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
IPR034099Small nuclear ribonucleoprotein Sm D3Family
IPR001163Sm domain, eukaryotic/archaea-typeDomain
IPR047575Sm domainDomain
IPR010920LSM domain superfamilyHomologous Superfamily
IPR022075Symplekin C-terminalDomain
IPR016024Armadillo-type foldHomologous Superfamily
IPR021850Symplekin/Pta1Family
IPR032460Symplekin/Pta1, N-terminalDomain
IPR011989Armadillo-like helicalHomologous Superfamily
IPR001163Sm domain, eukaryotic/archaea-typeDomain
IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
IPR047575Sm domainDomain
IPR010920LSM domain superfamilyHomologous Superfamily
C [auth F]IPR016487Sm-like protein Lsm6/SmFFamily
C [auth F]IPR034100Small nuclear ribonucleoprotein FFamily
C [auth F]IPR001163Sm domain, eukaryotic/archaea-typeDomain
C [auth F]IPR047575Sm domainDomain
C [auth F]IPR010920LSM domain superfamilyHomologous Superfamily
D [auth E]IPR027078Small nuclear ribonucleoprotein EFamily
D [auth E]IPR001163Sm domain, eukaryotic/archaea-typeDomain
D [auth E]IPR047575Sm domainDomain
D [auth E]IPR010920LSM domain superfamilyHomologous Superfamily
F [auth C]IPR001163Sm domain, eukaryotic/archaea-typeDomain
F [auth C]IPR047575Sm domainDomain
F [auth C]IPR010920LSM domain superfamilyHomologous Superfamily
G [auth D]IPR001163Sm domain, eukaryotic/archaea-typeDomain
G [auth D]IPR047575Sm domainDomain
G [auth D]IPR039267U7 snRNA-associated Sm-like protein Lsm11Family
G [auth D]IPR034109Sm-like protein Lsm11, middle domainDomain
G [auth D]IPR010920LSM domain superfamilyHomologous Superfamily
IPR001279Metallo-beta-lactamaseDomain
IPR022712Beta-Casp domainDomain
IPR027075Cleavage and polyadenylation specificity factor subunit 2Family
IPR011108Zn-dependent metallo-hydrolase, RNA specificity domainDomain
IPR036866Ribonuclease Z/Hydroxyacylglutathione hydrolase-likeHomologous Superfamily
IPR025069Cleavage and polyadenylation specificity factor 2, C-terminalDomain
IPR035639CPSF2, metallo-hydrolase domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
E [auth G]PharosP62308
PharosQ9UKF6
PharosP62318
PharosQ92797
PharosP14678
C [auth F]PharosP62306
D [auth E]PharosP62304
F [auth C]PharosQ969L4
G [auth D]PharosP83369
PharosQ9P2I0