6QW6

Structure of the human U5.U4/U6 tri-snRNP at 2.9A resolution.

External Resource: Annotation


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
U [auth 5D]SCOP2B SuperfamilyThioredoxin-like8044390 3000031 SCOP2B (2022-06-29)
GA [auth 65]SCOP2B SuperfamilySm-like ribonucleoproteins8063472 3000419 SCOP2B (2022-06-29)
Y [auth 5b]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
J [auth 4b]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
K [auth 4e]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
Z [auth 5e]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
AA [auth 5f]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
L [auth 4f]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
BA [auth 5g]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
M [auth 4g]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
R [auth 5A]SCOP2B SuperfamilyRibonuclease H-like8041105 3000143 SCOP2B (2022-06-29)
R [auth 5A]SCOP2B SuperfamilyJAB1/MPN domain-like8053277 3001105 SCOP2B (2022-06-29)
S [auth 5B]SCOP2B SuperfamilyE set domains8055093 3000070 SCOP2B (2022-06-29)
S [auth 5B]SCOP2B SuperfamilyBrl domain-like8036193 3000115 SCOP2B (2022-06-29)
EA [auth 63]SCOP2B SuperfamilySm-like ribonucleoproteins8063456 3000419 SCOP2B (2022-06-29)
FA [auth 64]SCOP2B SuperfamilySm-like ribonucleoproteins8063488 3000419 SCOP2B (2022-06-29)
HA [auth 66]SCOP2B SuperfamilySm-like ribonucleoproteins8063442 3000419 SCOP2B (2022-06-29)
IA [auth 67]SCOP2B SuperfamilySm-like ribonucleoproteins8063466 3000419 SCOP2B (2022-06-29)
JA [auth 68]SCOP2B SuperfamilySm-like ribonucleoproteins8063492 3000419 SCOP2B (2022-06-29)
C [auth 41]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
O [auth 51]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
D [auth 42]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
P [auth 52]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
E [auth 43]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
Q [auth 53]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
H [auth 4C]SCOP2B SuperfamilyNop domain8033305 3001551 SCOP2B (2022-06-29)
I [auth 4D]SCOP2B SuperfamilyL30e-like8043738 3001739 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
T [auth 5C]PF03144e6qw65C3 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF03144ECOD (1.6)
T [auth 5C]PF03764e6qw65C5 A: a+b two layersX: Ribosomal protein S5 domain 2-like (From Topology)H: Ribosomal protein S5 domain 2-like (From Topology)T: Ribosomal protein S5 domain 2-likeF: PF03764ECOD (1.6)
T [auth 5C]PF00679e6qw65C4 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: PF00679ECOD (1.6)
T [auth 5C]PF14492e6qw65C1 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: PF14492ECOD (1.6)
T [auth 5C]PF00009e6qw65C2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00009ECOD (1.6)
U [auth 5D]PF02966e6qw65D1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PF02966ECOD (1.6)
DA [auth 62]PF01423e6qw6621 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
GA [auth 65]PF01423e6qw6651 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Y [auth 5b]PF01423e6qw65b1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
J [auth 4b]PF01423e6qw64b1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
K [auth 4e]PF01423e6qw64e1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Z [auth 5e]PF01423e6qw65e1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
AA [auth 5f]PF01423e6qw65f1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
L [auth 4f]PF01423e6qw64f1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BA [auth 5g]PF01423e6qw65g1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
M [auth 4g]PF01423e6qw64g1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
R [auth 5A]PF10596,PF10597e6qw65A3 A: alpha bundlesX: helical bundle domain in reverse transcriptase-like polymerases (From Topology)H: helical bundle domain in reverse transcriptase-like polymerases (From Topology)T: helical bundle domain in reverse transcriptase-like polymerasesF: PF10596,PF10597ECOD (1.6)
R [auth 5A]PF08082,PF08083e6qw65A1 A: alpha complex topologyX: Pre-mRNA-splicing factor 8 N-terminal domain (From Topology)H: Pre-mRNA-splicing factor 8 N-terminal domain (From Topology)T: Pre-mRNA-splicing factor 8 N-terminal domainF: PF08082,PF08083ECOD (1.6)
R [auth 5A]PF10598e6qw65A6 A: a+b two layersX: Alpha-beta plaitsH: Adenylyl and guanylyl cyclase catalytic domain-likeT: Adenylyl and guanylyl cyclase catalytic domain-likeF: PF10598ECOD (1.6)
R [auth 5A]PF01398,PF08084e6qw65A4 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398,PF08084ECOD (1.6)
R [auth 5A]PF10596e6qw65A2 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
R [auth 5A]PF12134e6qw65A5 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
W [auth 5O]PF00400e6qw65O1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
EA [auth 63]PF01423e6qw6631 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
FA [auth 64]PF01423e6qw6641 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
HA [auth 66]PF01423e6qw6661 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
IA [auth 67]PF01423e6qw6671 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
JA [auth 68]PF01423e6qw6681 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
C [auth 41]PF01423e6qw6411 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
O [auth 51]PF01423e6qw6511 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
KA [auth R]PF00076e6qw6R1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
MA [auth U]PF00443e6qw6U2 A: a+b complex topologyX: Cysteine proteinases-likeH: Cysteine proteinases (From Topology)T: Cysteine proteinasesF: PF00443ECOD (1.6)
MA [auth U]PF02148e6qw6U1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: RING/U-boxF: PF02148ECOD (1.6)
D [auth 42]PF01423e6qw6421 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
P [auth 52]PF01423e6qw6521 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
E [auth 43]PF01423e6qw6431 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Q [auth 53]PF01423e6qw6531 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
F [auth 4A]PF06544e6qw64A2 A: a+b two layersX: Alpha-beta plaitsH: Acylphosphatase-like (From Topology)T: Acylphosphatase-likeF: PF06544ECOD (1.6)
F [auth 4A]PF08572e6qw64A1 A: extended segmentsX: U4/U6 small nuclear ribonucleoprotein PRP3 N-terminal region (From Topology)H: U4/U6 small nuclear ribonucleoprotein PRP3 N-terminal region (From Topology)T: U4/U6 small nuclear ribonucleoprotein PRP3 N-terminal regionF: PF08572ECOD (1.6)
G [auth 4B]PF00400e6qw64B1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
H [auth 4C]PF01798e6qw64C1 A: alpha arraysX: HhH/H2THH: SAM/DNA-glycosylaseT: Nop C-terminal domainF: PF01798ECOD (1.6)
H [auth 4C]PF01798e6qw64C2 A: alpha complex topologyX: Nop N-terminal domain (From Topology)H: Nop N-terminal domain (From Topology)T: Nop N-terminal domainF: PF01798ECOD (1.6)
H [auth 4C]PF09785e6qw64C3 A: extended segmentsX: Pre-mRNA-processing factor 31 C-terminal region (From Topology)H: Pre-mRNA-processing factor 31 C-terminal region (From Topology)T: Pre-mRNA-processing factor 31 C-terminal regionF: PF09785ECOD (1.6)
I [auth 4D]PF01248e6qw64D1 A: a+b three layersX: Bacillus chorismate mutase-likeH: L30e-like (From Topology)T: L30e-likeF: PF01248ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
T [auth 5C]PF00679Elongation factor G C-terminus (EFG_C)Elongation factor G C-terminusThis domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.Domain
T [auth 5C]PF00009Elongation factor Tu GTP binding domain (GTP_EFTU)Elongation factor Tu GTP binding domainThis domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.Domain
T [auth 5C]PF14492Elongation Factor G, domain III (EFG_III)Elongation Factor G, domain IIIThis domain is found in Elongation Factor G. It shares a similar structure with domain V (Pfam:PF00679). Structural studies in drosophila indicate this is domain 3 [1].Domain
T [auth 5C]PF16004116 kDa U5 small nuclear ribonucleoprotein component N-terminus (EFTUD2)116 kDa U5 small nuclear ribonucleoprotein component N-terminus- Family
T [auth 5C]PF03144Elongation factor Tu domain 2 (GTP_EFTU_D2)Elongation factor Tu domain 2Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.
Domain
T [auth 5C]PF03764Elongation factor G, domain IV (EFG_IV)Elongation factor G, domain IVThis domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.Domain
U [auth 5D]PF02966Mitosis protein DIM1 (DIM1)Mitosis protein DIM1- Domain
V [auth 5J]PF14559Tetratricopeptide repeat (TPR_19)Tetratricopeptide repeat- Repeat
V [auth 5J]PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
X [auth 5X]PF00270DEAD/DEAH box helicase (DEAD)DEAD/DEAH box helicaseMembers of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome ...Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Domain
X [auth 5X]PF00271Helicase conserved C-terminal domain (Helicase_C)Helicase conserved C-terminal domainThe Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.Domain
DA [auth 62]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
GA [auth 65]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
LA [auth S]PF03343SART-1 family (SART-1)SART-1 family- Family
A [auth X]PF08648U4/U6.U5 small nuclear ribonucleoproteins (SNRNP27)U4/U6.U5 small nuclear ribonucleoproteins- Family
J [auth 4b],
Y [auth 5b]		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
K [auth 4e],
Z [auth 5e]		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
AA [auth 5f],
L [auth 4f]		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
BA [auth 5g],
M [auth 4g]		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
R [auth 5A]PF10597U5-snRNA binding site 2 of PrP8 (U5_2-snRNA_bdg)U5-snRNA binding site 2 of PrP8The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis [1]. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that ...The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis [1]. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that Prp8 could directly affect the function of the catalytic core, perhaps acting as a splicing cofactor [2].
Domain
R [auth 5A]PF10598RNA recognition motif of the spliceosomal PrP8 (RRM_4)RNA recognition motif of the spliceosomal PrP8The large RNA-protein complex of the spliceosome catalyses pre-mRNA splicing. One of the most conserved core proteins is PrP8 which occupies a central position in the catalytic core of the spliceosome, and has been implicated in several crucial molec ...The large RNA-protein complex of the spliceosome catalyses pre-mRNA splicing. One of the most conserved core proteins is PrP8 which occupies a central position in the catalytic core of the spliceosome, and has been implicated in several crucial molecular rearrangements that occur there, and has recently come under the spotlight for its role in the inherited human disease, Retinitis Pigmentosa [1]. The RNA-recognition motif of PrP8 is highly conserved and provides a possible RNA binding centre for the 5-prime SS, BP, or 3-prime SS of pre-mRNA which are known to contact with Prp8. The most conserved regions of an RRM are defined as the RNP1 and RNP2 sequences. Recognition of RNA targets can also be modulated by a number of other factors, most notably the two loops beta1-alpha1, beta2-beta3 and the amino acid residues C-terminal to the RNP2 domain [2].
Domain
R [auth 5A]PF10596U6-snRNA interacting domain of PrP8 (U6-snRNA_bdg)U6-snRNA interacting domain of PrP8This domain incorporates the interacting site for the U6-snRNA as part of the U4/U6.U5 tri-snRNPs complex of the spliceosome, and is the prime candidate for the role of cofactor for the spliceosome's RNA core. The essential spliceosomal protein Prp8 ...This domain incorporates the interacting site for the U6-snRNA as part of the U4/U6.U5 tri-snRNPs complex of the spliceosome, and is the prime candidate for the role of cofactor for the spliceosome's RNA core. The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that Prp8 could directly affect the function of the catalytic core, perhaps acting as a splicing cofactor [1].
Domain
R [auth 5A]PF12134PRP8 domain IV core (PRP8_domainIV)PRP8 domain IV coreThis domain is found in eukaryotes, and is about 20 amino acids in length. It is found associated with Pfam:PF10597, Pfam:PF10596, Pfam:PF10598, Pfam:PF08083, Pfam:PF08082, Pfam:PF01398, Pfam:PF08084. There is a conserved LILR sequence motif. The dom ...This domain is found in eukaryotes, and is about 20 amino acids in length. It is found associated with Pfam:PF10597, Pfam:PF10596, Pfam:PF10598, Pfam:PF08083, Pfam:PF08082, Pfam:PF01398, Pfam:PF08084. There is a conserved LILR sequence motif. The domain is a selenomethionine domain in a subunit of the spliceosome. The function of PRP8 domain IV is believed to be interaction with the splicosomal core.
Domain
R [auth 5A]PF08082PRO8NT (NUC069), PrP8 N-terminal domain (PRO8NT)PRO8NT (NUC069), PrP8 N-terminal domainThe PRO8NT domain is found at the N-terminus of pre-mRNA splicing factors of PRO8 family [1]. The NLS or nuclear localisation signal for these spliceosome proteins begins at the start and runs for 60 residues. N-terminal to this domain is a highly va ...The PRO8NT domain is found at the N-terminus of pre-mRNA splicing factors of PRO8 family [1]. The NLS or nuclear localisation signal for these spliceosome proteins begins at the start and runs for 60 residues. N-terminal to this domain is a highly variable proline-rich region [4].
Domain
R [auth 5A]PF08083PROCN (NUC071) domain (PROCN)PROCN (NUC071) domainThe PROCN domain is the central domain in pre-mRNA splicing factors of PRO8 family [1].Domain
R [auth 5A]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
R [auth 5A]PF08084PROCT (NUC072) domain (PROCT)PROCT (NUC072) domainThe PROCT domain is the C-terminal domain in pre-mRNA splicing factors of PRO8 family [1].Domain
S [auth 5B]PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
S [auth 5B]PF21188Pre-mRNA-splicing helicase BRR2 plug domain (BRR2_plug)Pre-mRNA-splicing helicase BRR2 plug domainThis entry represents the Plug domain from the Brr2 RNA helicase protein. The Brr2 helicase provides the key remodelling activity for spliceosome catalytic activation, during which it disrupts the U4/U6 di-snRNP (small nuclear RNA protein) [2]. The p ...This entry represents the Plug domain from the Brr2 RNA helicase protein. The Brr2 helicase provides the key remodelling activity for spliceosome catalytic activation, during which it disrupts the U4/U6 di-snRNP (small nuclear RNA protein) [2]. The plug domain is a small alpha helical bundle domain found near the N-terminus of the Brr2 protein [2].
Domain
S [auth 5B]PF00270DEAD/DEAH box helicase (DEAD)DEAD/DEAH box helicaseMembers of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome ...Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Domain
S [auth 5B]PF00271Helicase conserved C-terminal domain (Helicase_C)Helicase conserved C-terminal domainThe Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.Domain
W [auth 5O]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
EA [auth 63]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
FA [auth 64]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
HA [auth 66]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
IA [auth 67]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
JA [auth 68]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 41],
O [auth 51]		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
KA [auth R]PF00076RNA recognition motif (RRM_1)RNA recognition motifThe RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and pro ...The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.
Domain
MA [auth U]PF02148Zn-finger in ubiquitin-hydrolases and other protein (zf-UBP)Zn-finger in ubiquitin-hydrolases and other protein- Domain
MA [auth U]PF00443Ubiquitin carboxyl-terminal hydrolase (UCH)Ubiquitin carboxyl-terminal hydrolase- Family
D [auth 42],
P [auth 52]		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
E [auth 43],
Q [auth 53]		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 4A]PF08572pre-mRNA processing factor 3 domain (PRP3)pre-mRNA processing factor 3 domainThis domain is found in U4/U6 and U4/U5/U6-small nuclear ribonucleoprotein Prp3, part of the tri-RNA complex that form the spliceosome. Prp3 plays a key role in the recognition of the snRNA duplex. The pre-mRNA processing factor 3 (PRP3) domain, resp ...This domain is found in U4/U6 and U4/U5/U6-small nuclear ribonucleoprotein Prp3, part of the tri-RNA complex that form the spliceosome. Prp3 plays a key role in the recognition of the snRNA duplex. The pre-mRNA processing factor 3 (PRP3) domain, responsible for the binding to stem II of the snRNA duplex, is highly conserved among eukaryotes and is found N-terminal to Pfam:PF06544 [3,4]. The human PRP3 has been implicated in autosomal retinitis pigmentosa [2].
Domain
F [auth 4A]PF06544Small nuclear ribonucleoprotein Prp3, C-terminal domain (Prp3_C)Small nuclear ribonucleoprotein Prp3, C-terminal domainThis domain is found at the C-terminal end of U4/U6 and U4/U5/U6- small nuclear ribonucleoprotein Prp3, part of the tri-RNA complex that form the spliceosome. Prp3 plays a key role in the recognition of the snRNA duplex. This binding domain, highly c ...This domain is found at the C-terminal end of U4/U6 and U4/U5/U6- small nuclear ribonucleoprotein Prp3, part of the tri-RNA complex that form the spliceosome. Prp3 plays a key role in the recognition of the snRNA duplex. This binding domain, highly conserved among eukaryotes, interacts with the 3' end of U6 snRNA. It adopts a ferredoxin-like fold, showing a five-stranded mixed beta-sheet with three alpha-helices, two of them running parallel to the beta-strands on one side of the sheet and one on the other. This fold is extended with a long beta-hairpin, an extra beta-strand, an helix and a final loop at the C terminus. It is located C-terminal to Pfam:PF08572 [1-4].
Domain
G [auth 4B]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
H [auth 4C]PF01798snoRNA binding domain, fibrillarin (Nop)snoRNA binding domain, fibrillarin- Family
I [auth 4D]PF01248Ribosomal protein L7Ae/L30e/S12e/Gadd45 family (Ribosomal_L7Ae)Ribosomal protein L7Ae/L30e/S12e/Gadd45 familyThis family includes: Ribosomal L7A from metazoa, Ribosomal L8-A and L8-B from fungi, 30S ribosomal protein HS6 from archaebacteria, 40S ribosomal protein S12 from eukaryotes, Ribosomal protein L30 from eukaryotes and archaebacteria. Gadd45 and MyD11 ...This family includes: Ribosomal L7A from metazoa, Ribosomal L8-A and L8-B from fungi, 30S ribosomal protein HS6 from archaebacteria, 40S ribosomal protein S12 from eukaryotes, Ribosomal protein L30 from eukaryotes and archaebacteria. Gadd45 and MyD118 [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
B [auth 4]U4 snRNA---
T [auth 5C]116 kDa U5 small nuclear ribonucleoprotein component
U [auth 5D]Thioredoxin-like protein 4A-
V [auth 5J]Pre-mRNA-processing factor 6
X [auth 5X]Probable ATP-dependent RNA helicase DDX23
CA [auth 6]U6 snRNA---
DA [auth 62]U6 snRNA-associated Sm-like protein LSm2
GA [auth 65]U6 snRNA-associated Sm-like protein LSm5
LA [auth S]U4/U6.U5 tri-snRNP-associated protein 1
A [auth X]U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein
J [auth 4b],
Y [auth 5b]		Small nuclear ribonucleoprotein-associated proteins B and B'
K [auth 4e],
Z [auth 5e]		Small nuclear ribonucleoprotein E
AA [auth 5f],
L [auth 4f]		Small nuclear ribonucleoprotein F
BA [auth 5g],
M [auth 4g]		Small nuclear ribonucleoprotein G
N [auth 5]U5 snRNA---
R [auth 5A]Pre-mRNA-processing-splicing factor 8
S [auth 5B]U5 small nuclear ribonucleoprotein 200 kDa helicase
W [auth 5O]U5 small nuclear ribonucleoprotein 40 kDa protein
EA [auth 63]U6 snRNA-associated Sm-like protein LSm3
FA [auth 64]U6 snRNA-associated Sm-like protein LSm4
HA [auth 66]U6 snRNA-associated Sm-like protein LSm6
IA [auth 67]U6 snRNA-associated Sm-like protein LSm7
JA [auth 68]U6 snRNA-associated Sm-like protein LSm8
C [auth 41],
O [auth 51]		Small nuclear ribonucleoprotein Sm D1
KA [auth R]RNA-binding protein 42
MA [auth U]U4/U6.U5 tri-snRNP-associated protein 2
D [auth 42],
P [auth 52]		Small nuclear ribonucleoprotein Sm D2
E [auth 43],
Q [auth 53]		Small nuclear ribonucleoprotein Sm D3
F [auth 4A]U4/U6 small nuclear ribonucleoprotein Prp3
G [auth 4B]U4/U6 small nuclear ribonucleoprotein Prp4
H [auth 4C]U4/U6 small nuclear ribonucleoprotein Prp31
I [auth 4D]NHP2-like protein 1

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
T [auth 5C]IPR005517Translation elongation factor EFG/EF2, domain IVDomain
T [auth 5C]IPR000795Translational (tr)-type GTP-binding domainDomain
T [auth 5C]IPR035647EF-G domain III/V-likeHomologous Superfamily
T [auth 5C]IPR035655116kDa U5 small nuclear ribonucleoprotein component, C-terminalDomain
T [auth 5C]IPR041095Elongation Factor G, domain IIDomain
T [auth 5C]IPR004161Translation elongation factor EFTu-like, domain 2Domain
T [auth 5C]IPR009000Translation protein, beta-barrel domain superfamilyHomologous Superfamily
T [auth 5C]IPR020568Ribosomal protein uS5 domain 2-type superfamilyHomologous Superfamily
T [auth 5C]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
T [auth 5C]IPR014721Small ribosomal subunit protein uS5 domain 2-type fold, subgroupHomologous Superfamily
T [auth 5C]IPR031950116kDa U5 small nuclear ribonucleoprotein component, N-terminalDomain
T [auth 5C]IPR000640Elongation factor EFG, domain V-likeDomain
T [auth 5C]IPR044121Snu114, GTP-binding domainDomain
T [auth 5C]IPR005225Small GTP-binding protein domainDomain
U [auth 5D]IPR004123Dim1 familyFamily
U [auth 5D]IPR036249Thioredoxin-like superfamilyHomologous Superfamily
V [auth 5J]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
V [auth 5J]IPR010491PRP1 splicing factor, N-terminalDomain
V [auth 5J]IPR003107HAT (Half-A-TPR) repeatRepeat
V [auth 5J]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
V [auth 5J]IPR019734Tetratricopeptide repeatRepeat
X [auth 5X]IPR001650Helicase, C-terminal domain-likeDomain
X [auth 5X]IPR000629ATP-dependent RNA helicase DEAD-box, conserved siteConserved Site
X [auth 5X]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
X [auth 5X]IPR014014RNA helicase, DEAD-box type, Q motifDomain
X [auth 5X]IPR011545DEAD/DEAH box helicase domainDomain
X [auth 5X]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
DA [auth 62]IPR001163Sm domain, eukaryotic/archaea-typeDomain
DA [auth 62]IPR047575Sm domainDomain
DA [auth 62]IPR010920LSM domain superfamilyHomologous Superfamily
DA [auth 62]IPR016654U6 snRNA-associated Sm-like protein LSm2Family
GA [auth 65]IPR001163Sm domain, eukaryotic/archaea-typeDomain
GA [auth 65]IPR047575Sm domainDomain
GA [auth 65]IPR033871Sm-like protein LSm5Domain
GA [auth 65]IPR010920LSM domain superfamilyHomologous Superfamily
LA [auth S]IPR045347HIND motifConserved Site
LA [auth S]IPR005011SNU66/SART1 familyFamily
A [auth X]IPR013957U4/U6.U5 small nuclear ribonucleoprotein 27kDa proteinDomain
J [auth 4b],
Y [auth 5b]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
J [auth 4b],
Y [auth 5b]		IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
J [auth 4b],
Y [auth 5b]		IPR047575Sm domainDomain
J [auth 4b],
Y [auth 5b]		IPR010920LSM domain superfamilyHomologous Superfamily
K [auth 4e],
Z [auth 5e]		IPR027078Small nuclear ribonucleoprotein EFamily
K [auth 4e],
Z [auth 5e]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
K [auth 4e],
Z [auth 5e]		IPR047575Sm domainDomain
K [auth 4e],
Z [auth 5e]		IPR010920LSM domain superfamilyHomologous Superfamily
AA [auth 5f],
L [auth 4f]		IPR016487Sm-like protein Lsm6/SmFFamily
AA [auth 5f],
L [auth 4f]		IPR034100Small nuclear ribonucleoprotein FFamily
AA [auth 5f],
L [auth 4f]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
AA [auth 5f],
L [auth 4f]		IPR047575Sm domainDomain
AA [auth 5f],
L [auth 4f]		IPR010920LSM domain superfamilyHomologous Superfamily
BA [auth 5g],
M [auth 4g]		IPR044641Sm-like protein Lsm7/SmGFamily
BA [auth 5g],
M [auth 4g]		IPR034098Small nuclear ribonucleoprotein GFamily
BA [auth 5g],
M [auth 4g]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
BA [auth 5g],
M [auth 4g]		IPR047575Sm domainDomain
BA [auth 5g],
M [auth 4g]		IPR010920LSM domain superfamilyHomologous Superfamily
R [auth 5A]IPR012984PROCT domainDomain
R [auth 5A]IPR012591PRO8NT domainDomain
R [auth 5A]IPR019580Pre-mRNA-processing-splicing factor 8, U6-snRNA-bindingDomain
R [auth 5A]IPR027652Pre-mRNA-processing-splicing factor 8Family
R [auth 5A]IPR043172Prp8 RNase domain IV, palm regionHomologous Superfamily
R [auth 5A]IPR012592PROCN domainDomain
R [auth 5A]IPR012337Ribonuclease H-like superfamilyHomologous Superfamily
R [auth 5A]IPR043173Prp8 RNase domain IV, fingers regionHomologous Superfamily
R [auth 5A]IPR021983PRP8 domain IV coreDomain
R [auth 5A]IPR019581Pre-mRNA-processing-splicing factor 8, U5-snRNA-bindingDomain
R [auth 5A]IPR037518MPN domainDomain
R [auth 5A]IPR019582RNA recognition motif, spliceosomal PrP8Domain
R [auth 5A]IPR042516Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamilyHomologous Superfamily
R [auth 5A]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
S [auth 5B]IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
S [auth 5B]IPR041094Brr2, N-terminal helicase PWI domainDomain
S [auth 5B]IPR004179Sec63 domainDomain
S [auth 5B]IPR014756Immunoglobulin E-setHomologous Superfamily
S [auth 5B]IPR011545DEAD/DEAH box helicase domainDomain
S [auth 5B]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
S [auth 5B]IPR001650Helicase, C-terminal domain-likeDomain
S [auth 5B]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
S [auth 5B]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
S [auth 5B]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
S [auth 5B]IPR035892C2 domain superfamilyHomologous Superfamily
W [auth 5O]IPR019775WD40 repeat, conserved siteConserved Site
W [auth 5O]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
W [auth 5O]IPR001680WD40 repeatRepeat
W [auth 5O]IPR020472G-protein beta WD-40 repeatRepeat
W [auth 5O]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
EA [auth 63]IPR040002U6 snRNA-associated Sm-like protein Lsm3Family
EA [auth 63]IPR001163Sm domain, eukaryotic/archaea-typeDomain
EA [auth 63]IPR047575Sm domainDomain
EA [auth 63]IPR010920LSM domain superfamilyHomologous Superfamily
EA [auth 63]IPR034105Sm-like protein Lsm3Domain
FA [auth 64]IPR001163Sm domain, eukaryotic/archaea-typeDomain
FA [auth 64]IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
FA [auth 64]IPR047575Sm domainDomain
FA [auth 64]IPR034101Sm-like protein Lsm4Domain
FA [auth 64]IPR010920LSM domain superfamilyHomologous Superfamily
HA [auth 66]IPR001163Sm domain, eukaryotic/archaea-typeDomain
HA [auth 66]IPR047575Sm domainDomain
HA [auth 66]IPR016487Sm-like protein Lsm6/SmFFamily
HA [auth 66]IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth 67]IPR001163Sm domain, eukaryotic/archaea-typeDomain
IA [auth 67]IPR047575Sm domainDomain
IA [auth 67]IPR044641Sm-like protein Lsm7/SmGFamily
IA [auth 67]IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth 67]IPR017132Sm-like protein Lsm7Family
JA [auth 68]IPR001163Sm domain, eukaryotic/archaea-typeDomain
JA [auth 68]IPR047575Sm domainDomain
JA [auth 68]IPR034103Sm-like protein Lsm8Domain
JA [auth 68]IPR010920LSM domain superfamilyHomologous Superfamily
JA [auth 68]IPR044642U6 snRNA-associated Sm-like protein Lsm1/8Family
C [auth 41],
O [auth 51]		IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
C [auth 41],
O [auth 51]		IPR034102Small nuclear ribonucleoprotein D1Domain
C [auth 41],
O [auth 51]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
C [auth 41],
O [auth 51]		IPR047575Sm domainDomain
C [auth 41],
O [auth 51]		IPR010920LSM domain superfamilyHomologous Superfamily
KA [auth R]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
KA [auth R]IPR034215RBM42, RNA recognition motifDomain
KA [auth R]IPR000504RNA recognition motif domainDomain
KA [auth R]IPR035979RNA-binding domain superfamilyHomologous Superfamily
MA [auth U]IPR028889Ubiquitin specific protease domainDomain
MA [auth U]IPR033809USP39Family
MA [auth U]IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
MA [auth U]IPR001607Zinc finger, UBP-typeDomain
MA [auth U]IPR001394Peptidase C19, ubiquitin carboxyl-terminal hydrolaseDomain
MA [auth U]IPR038765Papain-like cysteine peptidase superfamilyHomologous Superfamily
D [auth 42],
P [auth 52]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
D [auth 42],
P [auth 52]		IPR047575Sm domainDomain
D [auth 42],
P [auth 52]		IPR027248Small nuclear ribonucleoprotein Sm D2Family
D [auth 42],
P [auth 52]		IPR010920LSM domain superfamilyHomologous Superfamily
E [auth 43],
Q [auth 53]		IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
E [auth 43],
Q [auth 53]		IPR034099Small nuclear ribonucleoprotein Sm D3Family
E [auth 43],
Q [auth 53]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
E [auth 43],
Q [auth 53]		IPR047575Sm domainDomain
E [auth 43],
Q [auth 53]		IPR010920LSM domain superfamilyHomologous Superfamily
F [auth 4A]IPR027104U4/U6 small nuclear ribonucleoprotein Prp3Family
F [auth 4A]IPR002483PWI domainDomain
F [auth 4A]IPR013881Pre-mRNA-splicing factor 3 domainDomain
F [auth 4A]IPR036483PWI domain superfamilyHomologous Superfamily
F [auth 4A]IPR010541Small nuclear ribonucleoprotein Prp3, C-terminal domainDomain
G [auth 4B]IPR019775WD40 repeat, conserved siteConserved Site
G [auth 4B]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
G [auth 4B]IPR036285PRP4-like superfamilyHomologous Superfamily
G [auth 4B]IPR014906Pre-mRNA processing factor 4 (PRP4)-likeDomain
G [auth 4B]IPR001680WD40 repeatRepeat
G [auth 4B]IPR020472G-protein beta WD-40 repeatRepeat
G [auth 4B]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
H [auth 4C]IPR042239Nop, C-terminal domainHomologous Superfamily
H [auth 4C]IPR019175Prp31 C-terminalDomain
H [auth 4C]IPR002687Nop domainDomain
H [auth 4C]IPR012976NOSICDomain
H [auth 4C]IPR027105U4/U6 small nuclear ribonucleoprotein Prp31Family
H [auth 4C]IPR036070Nop domain superfamilyHomologous Superfamily
I [auth 4D]IPR002415H/ACA ribonucleoprotein complex, subunit Nhp2-likeFamily
I [auth 4D]IPR029064Ribosomal protein eL30-like superfamilyHomologous Superfamily
I [auth 4D]IPR018492Ribosomal protein eL8/Nhp2 familyFamily
I [auth 4D]IPR004038Ribosomal protein eL8/eL30/eS12/Gadd45Domain
I [auth 4D]IPR004037Large ribosomal subunit protein eL8-like, conserved siteConserved Site

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
T [auth 5C]Pharos:  Q15029
U [auth 5D]Pharos:  P83876
V [auth 5J]Pharos:  O94906
X [auth 5X]Pharos:  Q9BUQ8
DA [auth 62]Pharos:  Q9Y333
GA [auth 65]Pharos:  Q9Y4Y9
LA [auth S]Pharos:  O43290
A [auth X]Pharos:  Q8WVK2
J [auth 4b],
Y [auth 5b]		Pharos:  P14678
K [auth 4e],
Z [auth 5e]		Pharos:  P62304
AA [auth 5f],
L [auth 4f]		Pharos:  P62306
BA [auth 5g],
M [auth 4g]		Pharos:  P62308
R [auth 5A]Pharos:  Q6P2Q9
S [auth 5B]Pharos:  O75643
W [auth 5O]Pharos:  Q96DI7
EA [auth 63]Pharos:  P62310
FA [auth 64]Pharos:  Q9Y4Z0
HA [auth 66]Pharos:  P62312
IA [auth 67]Pharos:  Q9UK45
JA [auth 68]Pharos:  O95777
C [auth 41],
O [auth 51]		Pharos:  P62314
KA [auth R]Pharos:  Q9BTD8
MA [auth U]Pharos:  Q53GS9
D [auth 42],
P [auth 52]		Pharos:  P62316
E [auth 43],
Q [auth 53]		Pharos:  P62318
F [auth 4A]Pharos:  O43395
G [auth 4B]Pharos:  O43172
H [auth 4C]Pharos:  Q8WWY3
I [auth 4D]Pharos:  P55769