5Z57

Cryo-EM structure of the human activated spliceosome (late Bact) at 6.5 angstrom


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyJAB1/MPN domain-like8053277 3001105 SCOP2B (2022-06-29)
J [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
T [auth m]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
K [auth e]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
U [auth l]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
L [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
V [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
W [auth o]SCOP2B SuperfamilyL domain-like8043993 3001010 SCOP2B (2022-06-29)
X [auth p]SCOP2B SuperfamilyRNA-binding domain RBD8035327 3000110 SCOP2B (2022-06-29)
DA [auth 3]SCOP2B SuperfamilyWD40 repeat-like8051197 3001694 SCOP2B (2022-06-29)
DA [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
DA [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
DA [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052535 3001694 SCOP2B (2022-06-29)
EA [auth 4]SCOP2B SuperfamilyRNA-binding domain RBD8090834 3000110 SCOP2B (2022-06-29)
FA [auth 5]SCOP2B SuperfamilyRNA-binding domain RBD8040695 3000110 SCOP2B (2022-06-29)
GA [auth 6]SCOP2B SuperfamilyTriquetra zinc finger motif8051848 3002040 SCOP2B (2022-06-29)
JA [auth L]SCOP2B SuperfamilyHomeodomain-like8089608 3000001 SCOP2B (2022-06-29)
QA [auth Q]SCOP2B SuperfamilyARM repeat-like8090869 3000116 SCOP2B (2022-06-29)
QA [auth Q]SCOP2B SuperfamilyRecA-like P-loop NTPases8090872 3002019 SCOP2B (2022-06-29)
QA [auth Q]SCOP2B SuperfamilyRecA-like P-loop NTPases8090871 3002019 SCOP2B (2022-06-29)
QA [auth Q]SCOP2B SuperfamilyUpf1 beta-barrel domain-like8090870 3002168 SCOP2B (2022-06-29)
SA [auth O]SCOP2B SuperfamilyRNA-binding domain RBD8064957 3000110 SCOP2B (2022-06-29)
VA [auth S]SCOP2B SuperfamilyCyclophilin-like8033930 3000168 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyBrl domain-like8036193 3000115 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyE set domains8055093 3000070 SCOP2B (2022-06-29)
BB [auth Y]SCOP2B SuperfamilyRNA-binding domain RBD8061967 3000110 SCOP2B (2022-06-29)
EB [auth y]SCOP2B SuperfamilyCyclophilin-like8035984 3000168 SCOP2B (2022-06-29)
EB [auth y]SCOP2B SuperfamilyRNA-binding domain RBD8039202 3000110 SCOP2B (2022-06-29)
P [auth h]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
F [auth a]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
G [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
Q [auth i]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
H [auth c]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
R [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
I [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
S [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AU5_2-snRNA_bdge5z57A3 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: U5_2-snRNA_bdgECOD (1.6)
APROCN_C,PROCN_Ne5z57A1 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: PROCN_C,PROCN_NECOD (1.6)
ARRM_4e5z57A2 A: a+b two layersX: Alpha-beta plaitsH: Adenylyl and guanylyl cyclase catalytic domain-likeT: Adenylyl and guanylyl cyclase catalytic domain-likeF: RRM_4ECOD (1.6)
APROCTe5z57A4 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PROCTECOD (1.6)
AU6-snRNA_bdge5z57A5 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: U6-snRNA_bdgECOD (1.6)
J [auth f]LSMe5z57f1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
T [auth m]LSMe5z57m1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
K [auth e]LSMe5z57e1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
U [auth l]LSMe5z57l1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
L [auth g]LSMe5z57g1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
V [auth n]LSMe5z57n1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
W [auth o]LRR_9e5z57o1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Leucine-rich repeats (From Topology)T: Leucine-rich repeatsF: LRR_9ECOD (1.6)
X [auth p]RRM_1_1e5z57p2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_1ECOD (1.6)
X [auth p]RRM_1_2e5z57p1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_2ECOD (1.6)
Y [auth w]PRP9_Ne5z57w1 A: alpha bundlesX: Pre-mRNA-splicing factor PRP9 (From Topology)H: Pre-mRNA-splicing factor PRP9 (From Topology)T: Pre-mRNA-splicing factor PRP9F: PRP9_NECOD (1.6)
Z [auth u]Surpe5z57u1 A: alpha bundlesX: Surp module (SWAP domain) (From Topology)H: Surp module (SWAP domain) (From Topology)T: Surp module (SWAP domain)F: SurpECOD (1.6)
AA [auth v]SF3A2e5z57v1 A: beta sandwichesX: HSP20-likeH: Pre-mRNA-splicing factor PRP11 C-terminal domain (From Topology)T: Pre-mRNA-splicing factor PRP11 C-terminal domainF: SF3A2ECOD (1.6)
AA [auth v]zf-met_1e5z57v2 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: zf-met_1ECOD (1.6)
BA [auth 1]KOG0213e5z5711 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG0213ECOD (1.6)
DA [auth 3]CPSF_A_Ne5z5732 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: CPSF_A_NECOD (1.6)
DA [auth 3]MMS1_N_Ce5z5734 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: MMS1_N_CECOD (1.6)
DA [auth 3]MMS1_N_Ne5z5731 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: MMS1_N_NECOD (1.6)
DA [auth 3]CPSF_A_Ce5z5733 A: alpha arraysX: HTHH: HTHT: tri-helicalF: CPSF_A_CECOD (1.6)
EA [auth 4]RRM_1_1e5z5741 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_1ECOD (1.6)
FA [auth 5]RRM_1_2e5z5751 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_2ECOD (1.6)
GA [auth 6]PHF5e5z5761 A: few secondary structure elementsX: Glucocorticoid receptor-likeH: LIM domain-likeT: PHD finger-like domain-containing protein 5AF: PHF5ECOD (1.6)
HA [auth 7]SF3b10e5z5771 A: alpha arraysX: RDS3 complex subunit 10 (From Topology)H: RDS3 complex subunit 10 (From Topology)T: RDS3 complex subunit 10F: SF3b10ECOD (1.6)
IA [auth J]TPR_11_6e5z57J1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_6ECOD (1.6)
PA [auth I]TPR_15e5z57I1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_15ECOD (1.6)
QA [auth Q]Aquarius_N_2nde5z57Q5 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: Aquarius_N_2ndECOD (1.6)
QA [auth Q]Aquarius_N_1ste5z57Q4 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: Aquarius_N_1stECOD (1.6)
QA [auth Q]Aquarius_N_3rde5z57Q2 A: a+b two layersX: Spliceosomal helicase Aquarius insert domain (From Topology)H: Spliceosomal helicase Aquarius insert domain (From Topology)T: Spliceosomal helicase Aquarius insert domainF: Aquarius_N_3rdECOD (1.6)
QA [auth Q]AAA_11_1e5z57Q1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_11_1ECOD (1.6)
QA [auth Q]AAA_12e5z57Q3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_12ECOD (1.6)
RA [auth N]G10e5z57N1 A: few secondary structure elementsX: Pre-mRNA-splicing factor BUD31 (From Topology)H: Pre-mRNA-splicing factor BUD31 (From Topology)T: Pre-mRNA-splicing factor BUD31F: G10ECOD (1.6)
SA [auth O]RRM_1_6e5z57O1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_6ECOD (1.6)
SA [auth O]KOG0153e5z57O2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: KOG0153ECOD (1.6)
SA [auth O]Toruse5z57O3 A: few secondary structure elementsX: CCCH zinc fingerH: CCCH zinc finger (From Topology)T: CCCH zinc fingerF: TorusECOD (1.6)
VA [auth S]Pro_isomerasee5z57S1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: Pro_isomeraseECOD (1.6)
WA [auth T]ANAPC4_WD40_1e5z57T1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: ANAPC4_WD40_1ECOD (1.6)
DSec63_3rde5z57D12 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: Sec63_3rdECOD (1.6)
DKOG0952e5z57D6 A: alpha arraysX: HTHH: HTHT: wingedF: KOG0952ECOD (1.6)
DSec63_2nd_1e5z57D8 A: alpha arraysX: HhH/H2THH: SAM-like subdomain in Sec63-like proteins (From Topology)T: SAM-like subdomain in Sec63-like proteinsF: Sec63_2nd_1ECOD (1.6)
DSec63_2nde5z57D2 A: alpha arraysX: HhH/H2THH: SAM-like subdomain in Sec63-like proteins (From Topology)T: SAM-like subdomain in Sec63-like proteinsF: Sec63_2ndECOD (1.6)
DSec63_1ste5z57D11 A: alpha arraysX: Sec63 N-terminal subdomain-like (From Topology)H: Sec63 N-terminal subdomain-like (From Topology)T: Sec63 N-terminal subdomain-likeF: Sec63_1stECOD (1.6)
DDEAD_1e5z57D5 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: DEAD_1ECOD (1.6)
DHelicase_C_5e5z57D1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Helicase_C_5ECOD (1.6)
DDEAD_1,KOG0951_2nde5z57D4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: DEAD_1,KOG0951_2ndECOD (1.6)
YA [auth V]MIF4Ge5z57V2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: MIF4GECOD (1.6)
YA [auth V]MA3e5z57V1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: MA3ECOD (1.6)
AB [auth X]FHAe5z57X1 A: beta sandwichesX: SMAD/FHA domain (From Topology)H: SMAD/FHA domain (From Topology)T: SMAD/FHA domainF: FHAECOD (1.6)
BB [auth Y]RRM_1_4e5z57Y1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_4ECOD (1.6)
DB [auth x]OB_NTP_binde5z57x3 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: OB_NTP_bindECOD (1.6)
DB [auth x]HA2_N,HA2_Ce5z57x1 A: alpha arraysX: Sec63 N-terminal subdomain-like (From Topology)H: Sec63 N-terminal subdomain-like (From Topology)T: Sec63 N-terminal subdomain-likeF: HA2_N,HA2_CECOD (1.6)
DB [auth x]Helicase_C_7e5z57x2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Helicase_C_7ECOD (1.6)
DB [auth x]DEAD_3e5z57x4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: DEAD_3ECOD (1.6)
EB [auth y]Pro_isomerasee5z57y1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: Pro_isomeraseECOD (1.6)
EB [auth y]RRM_1_1e5z57y2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_1ECOD (1.6)
EANAPC4_WD40_7e5z57E1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: ANAPC4_WD40_7ECOD (1.6)
P [auth h]LSMe5z57h1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
F [auth a]LSMe5z57a1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
G [auth b]LSMe5z57b1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
Q [auth i]LSMe5z57i1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
H [auth c]LSMe5z57c1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
R [auth j]LSMe5z57j1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
I [auth d]LSMe5z57d1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
S [auth k]LSMe5z57k1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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
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
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
PF08083PROCN (NUC071) domain (PROCN)PROCN (NUC071) domainThe PROCN domain is the central domain in pre-mRNA splicing factors of PRO8 family [1].Domain
PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
PF08084PROCT (NUC072) domain (PROCT)PROCT (NUC072) domainThe PROCT domain is the C-terminal domain in pre-mRNA splicing factors of PRO8 family [1].Domain
J [auth f],
T [auth m]
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 e],
U [auth l]
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
L [auth g],
V [auth n]
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
W [auth o]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
X [auth p]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
Y [auth w]PF16837Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9 (SF3A3)Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9SF3A3 is one of the components of the SF3a splicing factor complex of the mature U2 snRNP (small nuclear ribonucleoprotein particle). In yeast, SF3a shows a bifurcated assembly structure of three subunits, Prp9 (subunit 3), Prp11 (subunit 2) and Prp2 ...SF3A3 is one of the components of the SF3a splicing factor complex of the mature U2 snRNP (small nuclear ribonucleoprotein particle). In yeast, SF3a shows a bifurcated assembly structure of three subunits, Prp9 (subunit 3), Prp11 (subunit 2) and Prp21 (subunit 1). Prp9 and Prp21 were not thought to interact with each other but the alpha1 helix of Prp9 does make important contacts with the SURP2 domain of Prp21, thus the two do interact via a bidentate-binding mode. Prp9 harbours a major binding site for stem-loop IIa of U2 snRNA [1].
Domain
Y [auth w]PF13297Replication stress response SDE2 C-terminal (SDE2_2C)Replication stress response SDE2 C-terminalThis domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved fr ...This domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved from its N-terminal at a diglycine motif within the ubiquitin-like fold, after Proliferating cell nuclear antigen (PCNA) interaction. This generates a functional protein that negatively regulates damage-inducible PCNA monoubiquitination, which then is proteolytically degraded to allow S phase progression and replication fork recovery in response to DNA damage [1].
Domain
Z [auth u]PF01805Surp module (Surp)Surp module- Family
AA [auth v]PF12874Zinc-finger of C2H2 type (zf-met)Zinc-finger of C2H2 typeThis is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.Domain
CA [auth 2]PF04037Domain of unknown function (DUF382) (DUF382)Domain of unknown function (DUF382)- Family
CA [auth 2]PF04046PSP (PSP)PSP- Family
DA [auth 3]PF10433Mono-functional DNA-alkylating methyl methanesulfonate N-term (MMS1_N)Mono-functional DNA-alkylating methyl methanesulfonate N-term- Repeat
DA [auth 3]PF03178CPSF A subunit region (CPSF_A)CPSF A subunit region- Repeat
EA [auth 4]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
FA [auth 5]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
GA [auth 6]PF03660PHF5-like protein (PHF5)PHF5-like protein- Family
HA [auth 7]PF07189Splicing factor 3B subunit 10 (SF3b10) (SF3b10)Splicing factor 3B subunit 10 (SF3b10)- Family
IA [auth J]PF02184HAT (Half-A-TPR) repeat (HAT)HAT (Half-A-TPR) repeat- Repeat
JA [auth L]PF13921Myb-like DNA-binding domain (Myb_DNA-bind_6)Myb-like DNA-binding domainThis family contains the DNA binding domains from Myb proteins, as well as the SANT domain family [1].Domain
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
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
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
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
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
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
PF08606Prp19/Pso4-like (Prp19)Prp19/Pso4-likeThis regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif [1]. PRP19-like proteins form an oligomer that is necessary ...This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif [1]. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly [1].
Domain
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
PF04564U-box domain (U-box)U-box domainThe U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop ...The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process [1-3]. This domain is related to the Ring finger Pfam:PF00097 but lacks the zinc binding residues [4].
Domain
OA [auth K]PF05700Breast carcinoma amplified sequence 2 (BCAS2) (BCAS2)Breast carcinoma amplified sequence 2 (BCAS2)- Family
PA [auth I]PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
QA [auth Q]PF21144Intron-binding protein aquarius insert domain (Aquarius_N_3rd)Intron-binding protein aquarius insert domainThis entry represents the insert domain of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly [1,2].Domain
QA [auth Q]PF13086AAA domain (AAA_11)AAA domainThis family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.Domain
QA [auth Q]PF21143Intron-binding protein aquarius, beta-barrel (Aquarius_N_2nd)Intron-binding protein aquarius, beta-barrelThis entry represents the beta-barrel domain found at the N-terminal of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly [1,2].Domain
QA [auth Q]PF13087AAA domain (AAA_12)AAA domainThis family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.Domain
QA [auth Q]PF16399Intron-binding protein aquarius N-terminal (Aquarius_N_1st)Intron-binding protein aquarius N-terminal- Repeat
RA [auth N]PF01125Pre-mRNA-splicing factor BUD31 (BUD31)Pre-mRNA-splicing factor BUD31This entry includes Pre-mRNA-splicing factor BUD31, also known as G10 protein, and its homologues. BUD31 is involved in the pre-mRNA splicing process [1-3] and it is highly conserved in a wide range of eukaryotic species. Human BUD31 may play a role ...This entry includes Pre-mRNA-splicing factor BUD31, also known as G10 protein, and its homologues. BUD31 is involved in the pre-mRNA splicing process [1-3] and it is highly conserved in a wide range of eukaryotic species. Human BUD31 may play a role as a regulator of androgen receptor (AR) transcriptional activity, probably increasing the AR transcriptional activity [4].
Domain
SA [auth O]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
SA [auth O]PF21369STL11, N-terminal (STL11_N)STL11, N-terminalThis entry represents the N-terminal domain of STL11 from yeast and its homologues [1-4], such as RBM22 from human. This domain comprises a zinc finger, FYVE/PHD type. Members of this entry are involved in pre-mRNA splicing.Domain
TA [auth P]PF04889Cwf15/Cwc15 cell cycle control protein (Cwf_Cwc_15)Cwf15/Cwc15 cell cycle control protein- Family
VA [auth S]PF00160Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD (Pro_isomerase)Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDThe peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond pr ...The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function [1].
Domain
WA [auth T]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
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
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
YA [auth V]PF02854MIF4G domain (MIF4G)MIF4G domain- Repeat
ZA [auth W]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
BB [auth Y]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
CB [auth Z]PF09736Pre-mRNA-splicing factor of RES complex (Bud13)Pre-mRNA-splicing factor of RES complex- Family
DB [auth x]PF04408Helicase associated domain (HA2), winged-helix (HA2_N)Helicase associated domain (HA2), winged-helixThe helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains collaborate wit ...The helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains collaborate with RecA domains at the N-terminal in completing an RNA binding channel to allow the helicases to keep a stable grip on the RNA [3] and assure its correct function. This entry represents the WH domain, which connects the N- (RecA domains) and C-terminal domains (ratchet-like and OB-fold) of helicases.
Domain
DB [auth x]PF07717Oligonucleotide/oligosaccharide-binding (OB)-fold (OB_NTP_bind)Oligonucleotide/oligosaccharide-binding (OB)-foldThis family is found towards the C-terminus of the DEAD-box helicases (Pfam:PF00270). In these helicases it is apparently always found in association with Pfam:PF04408. There do seem to be a couple of instances where it occurs by itself - e.g. Swiss: ...This family is found towards the C-terminus of the DEAD-box helicases (Pfam:PF00270). In these helicases it is apparently always found in association with Pfam:PF04408. There do seem to be a couple of instances where it occurs by itself - e.g. Swiss:Q84VZ2. The structure PDB:3i4u adopts an OB-fold. helicases (Pfam:PF00270). In these helicases it is apparently always found in association with Pfam:PF04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins [1].
Domain
DB [auth x]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
DB [auth x]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
DB [auth x]PF21010Helicase associated domain (HA2), ratchet-like (HA2_C)Helicase associated domain (HA2), ratchet-likeThe helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain (Pfam:PF04408) and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains c ...The helicase associated domain (HA2) has an all alpha-helical fold and consists of a N-terminal winged-helix (WH) domain (Pfam:PF04408) and a C-terminal degenerate helical-bundle domain, referred to as the ratchet-like domain [1,2,3]. These domains collaborate with the RecA domains at the N-terminal in completing an RNA binding channel to allow the helicases to keep a stable grip on the RNA [3]. This entry represents the ratchet-like domain, which may be important for RNA translocation [1,2].
Domain
EB [auth y]PF00160Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD (Pro_isomerase)Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDThe peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond pr ...The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function [1].
Domain
EB [auth y]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
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
F [auth a],
P [auth h]
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
G [auth b],
Q [auth i]
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
H [auth c],
R [auth j]
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
I [auth d],
S [auth k]
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Pre-mRNA-processing-splicing factor 8
J [auth f],
T [auth m]
Small nuclear ribonucleoprotein F
K [auth e],
U [auth l]
Small nuclear ribonucleoprotein E
L [auth g],
V [auth n]
Small nuclear ribonucleoprotein G
M [auth F]U6 snRNA---
N [auth G]pre-mRNA---
O [auth H]U2 snRNA---
W [auth o]U2 small nuclear ribonucleoprotein A'
X [auth p]U2 small nuclear ribonucleoprotein B''
Y [auth w]Splicing factor 3A subunit 3
Z [auth u]Splicing factor 3A subunit 1
U5 snRNA---
AA [auth v]Splicing factor 3A subunit 2
BA [auth 1]Splicing factor 3B subunit 1
CA [auth 2]Splicing factor 3B subunit 2
DA [auth 3]Splicing factor 3B subunit 3
EA [auth 4]Splicing factor 3B subunit 4
FA [auth 5]Splicing factor 3B subunit 6
GA [auth 6]PHD finger-like domain-containing protein 5A
HA [auth 7]Splicing factor 3B subunit 5
IA [auth J]Crooked neck-like protein 1
JA [auth L]Cell division cycle 5-like protein
116 kDa U5 small nuclear ribonucleoprotein component
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
Pre-mRNA-processing factor 19
OA [auth K]Pre-mRNA-splicing factor SPF27-
PA [auth I]Pre-mRNA-splicing factor SYF1-
QA [auth Q]Intron-binding protein aquarius
RA [auth N]Protein BUD31 homolog
SA [auth O]Pre-mRNA-splicing factor RBM22
TA [auth P]Spliceosome-associated protein CWC15 homolog
UA [auth R]Skip---
VA [auth S]Peptidyl-prolyl cis-trans isomerase-like 1
WA [auth T]Pleiotropic regulator 1-
U5 small nuclear ribonucleoprotein 200 kDa helicase
XA [auth U]Serine/arginine repetitive matrix protein 2
YA [auth V]Pre-mRNA-splicing factor CWC22 homolog
ZA [auth W]Pre-mRNA-processing factor 17
AB [auth X]Smad nuclear-interacting protein 1
BB [auth Y]RNA-binding motif protein, X-linked 2
CB [auth Z]BUD13 homolog
DB [auth x]Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
EB [auth y]Peptidyl-prolyl cis-trans isomerase E
U5 small nuclear ribonucleoprotein 40 kDa protein
F [auth a],
P [auth h]
Small nuclear ribonucleoprotein Sm D3
G [auth b],
Q [auth i]
Small nuclear ribonucleoprotein-associated proteins B and B'
H [auth c],
R [auth j]
Small nuclear ribonucleoprotein Sm D1
I [auth d],
S [auth k]
Small nuclear ribonucleoprotein Sm D2

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR012984PROCT domainDomain
IPR012591PRO8NT domainDomain
IPR019580Pre-mRNA-processing-splicing factor 8, U6-snRNA-bindingDomain
IPR027652Pre-mRNA-processing-splicing factor 8Family
IPR043172Prp8 RNase domain IV, palm regionHomologous Superfamily
IPR012592PROCN domainDomain
IPR012337Ribonuclease H-like superfamilyHomologous Superfamily
IPR043173Prp8 RNase domain IV, fingers regionHomologous Superfamily
IPR021983PRP8 domain IV coreDomain
IPR019581Pre-mRNA-processing-splicing factor 8, U5-snRNA-bindingDomain
IPR037518MPN domainDomain
IPR019582RNA recognition motif, spliceosomal PrP8Domain
IPR042516Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamilyHomologous Superfamily
IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
J [auth f],
T [auth m]
IPR016487Sm-like protein Lsm6/SmFFamily
J [auth f],
T [auth m]
IPR034100Small nuclear ribonucleoprotein FFamily
J [auth f],
T [auth m]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
J [auth f],
T [auth m]
IPR047575Sm domainDomain
J [auth f],
T [auth m]
IPR010920LSM domain superfamilyHomologous Superfamily
K [auth e],
U [auth l]
IPR027078Small nuclear ribonucleoprotein EFamily
K [auth e],
U [auth l]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
K [auth e],
U [auth l]
IPR047575Sm domainDomain
K [auth e],
U [auth l]
IPR010920LSM domain superfamilyHomologous Superfamily
L [auth g],
V [auth n]
IPR044641Sm-like protein Lsm7/SmGFamily
L [auth g],
V [auth n]
IPR034098Small nuclear ribonucleoprotein GFamily
L [auth g],
V [auth n]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
L [auth g],
V [auth n]
IPR047575Sm domainDomain
L [auth g],
V [auth n]
IPR010920LSM domain superfamilyHomologous Superfamily
W [auth o]IPR001611Leucine-rich repeatRepeat
W [auth o]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
W [auth o]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
X [auth p]IPR034562U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2Domain
X [auth p]IPR000504RNA recognition motif domainDomain
X [auth p]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
X [auth p]IPR035979RNA-binding domain superfamilyHomologous Superfamily
X [auth p]IPR034564U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1Domain
Y [auth w]IPR021966Splicing factor SF3a60 binding domainDomain
Y [auth w]IPR031774SF3A3 domainDomain
Y [auth w]IPR024598Splicing factor SF3a60 /Prp9 subunit, C-terminalDomain
Y [auth w]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
Y [auth w]IPR025086SDE2-like, C-terminal domainDomain
Z [auth u]IPR045146Splicing factor 3A subunit 1Family
Z [auth u]IPR035967SWAP/Surp superfamilyHomologous Superfamily
Z [auth u]IPR000061SWAP/SurpDomain
Z [auth u]IPR000626Ubiquitin-like domainDomain
Z [auth u]IPR035563Splicing factor 3A subunit 1, ubiquitin domainDomain
Z [auth u]IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
Z [auth u]IPR022030Splicing factor 3A subunit 1, conserved domainDomain
AA [auth v]IPR031781SF3A2 domainDomain
AA [auth v]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
AA [auth v]IPR013087Zinc finger C2H2-typeDomain
AA [auth v]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
AA [auth v]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
BA [auth 1]IPR016024Armadillo-type foldHomologous Superfamily
BA [auth 1]IPR011989Armadillo-like helicalHomologous Superfamily
BA [auth 1]IPR015016Splicing factor 3B subunit 1Domain
BA [auth 1]IPR038737Splicing factor 3B subunit 1-likeFamily
CA [auth 2]IPR006568PSP, proline-richDomain
CA [auth 2]IPR007180Domain of unknown function DUF382Domain
CA [auth 2]IPR003034SAP domainDomain
DA [auth 3]IPR018846Cleavage/polyadenylation specificity factor, A subunit, N-terminalDomain
DA [auth 3]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
DA [auth 3]IPR004871Cleavage/polyadenylation specificity factor, A subunit, C-terminalDomain
DA [auth 3]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
EA [auth 4]IPR034159SF3B4, RNA recognition motif 2Domain
EA [auth 4]IPR000504RNA recognition motif domainDomain
EA [auth 4]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
EA [auth 4]IPR035979RNA-binding domain superfamilyHomologous Superfamily
EA [auth 4]IPR034158SF3B4, RNA recognition motif 1Domain
FA [auth 5]IPR000504RNA recognition motif domainDomain
FA [auth 5]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
FA [auth 5]IPR034150SF3B6, RNA recognition motifDomain
FA [auth 5]IPR035979RNA-binding domain superfamilyHomologous Superfamily
GA [auth 6]IPR005345PHF5-likeFamily
HA [auth 7]IPR017089Splicing factor 3B, subunit 5Family
HA [auth 7]IPR009846Splicing factor 3B subunit 5/RDS3 complex subunit 10Family
IA [auth J]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
IA [auth J]IPR003107HAT (Half-A-TPR) repeatRepeat
IA [auth J]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
JA [auth L]IPR047240Pre-mRNA splicing factor component CDC5L/Cef1, second SANT/myb-like domainDomain
JA [auth L]IPR017930Myb domainDomain
JA [auth L]IPR009057Homeobox-like domain superfamilyHomologous Superfamily
JA [auth L]IPR047242Pre-mRNA splicing factor component CDC5L/Cef1Family
JA [auth L]IPR001005SANT/Myb domainDomain
JA [auth L]IPR021786Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminalDomain
IPR005517Translation elongation factor EFG/EF2, domain IVDomain
IPR000795Translational (tr)-type GTP-binding domainDomain
IPR035647EF-G domain III/V-likeHomologous Superfamily
IPR035655116kDa U5 small nuclear ribonucleoprotein component, C-terminalDomain
IPR041095Elongation Factor G, domain IIDomain
IPR004161Translation elongation factor EFTu-like, domain 2Domain
IPR009000Translation protein, beta-barrel domain superfamilyHomologous Superfamily
IPR020568Ribosomal protein uS5 domain 2-type superfamilyHomologous Superfamily
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IPR014721Small ribosomal subunit protein uS5 domain 2-type fold, subgroupHomologous Superfamily
IPR031950116kDa U5 small nuclear ribonucleoprotein component, N-terminalDomain
IPR000640Elongation factor EFG, domain V-likeDomain
IPR044121Snu114, GTP-binding domainDomain
IPR005225Small GTP-binding protein domainDomain
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR013915Pre-mRNA-splicing factor 19Domain
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR019775WD40 repeat, conserved siteConserved Site
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR038959Pre-mRNA-processing factor 19Family
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR003613U-box domainDomain
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR001680WD40 repeatRepeat
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
IPR020472G-protein beta WD-40 repeatRepeat
OA [auth K]IPR008409Pre-mRNA-splicing factor SPF27Family
PA [auth I]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
PA [auth I]IPR003107HAT (Half-A-TPR) repeatRepeat
PA [auth I]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
PA [auth I]IPR019734Tetratricopeptide repeatRepeat
QA [auth Q]IPR048966RNA helicase aquarius, beta-barrelDomain
QA [auth Q]IPR048967RNA helicase aquarius, insertion domainDomain
QA [auth Q]IPR041677DNA2/NAM7 helicase, helicase domainDomain
QA [auth Q]IPR026300CWF11 familyFamily
QA [auth Q]IPR045055DNA2/NAM7-like helicaseFamily
QA [auth Q]IPR032174RNA helicase aquarius, N-terminal domainDomain
QA [auth Q]IPR041679DNA2/NAM7 helicase-like, C-terminalDomain
QA [auth Q]IPR047187Upf1-like, C-terminal helicase domainDomain
QA [auth Q]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
RA [auth N]IPR001748Pre-mRNA-splicing factor BUD31Family
RA [auth N]IPR018230BUD31/G10-related, conserved siteConserved Site
SA [auth O]IPR036855Zinc finger, CCCH-type superfamilyHomologous Superfamily
SA [auth O]IPR039171Pre-mRNA-splicing factor Cwc2/Slt11Family
SA [auth O]IPR000504RNA recognition motif domainDomain
SA [auth O]IPR000571Zinc finger, CCCH-typeDomain
SA [auth O]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
SA [auth O]IPR048995STL11/RBM22-like, N-terminal domainDomain
SA [auth O]IPR035979RNA-binding domain superfamilyHomologous Superfamily
TA [auth P]IPR006973Pre-mRNA-splicing factor Cwf15/Cwc15Family
VA [auth S]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
VA [auth S]IPR024936Cyclophilin-type peptidyl-prolyl cis-trans isomeraseFamily
VA [auth S]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
VA [auth S]IPR044666Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-likeFamily
VA [auth S]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
WA [auth T]IPR019775WD40 repeat, conserved siteConserved Site
WA [auth T]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
WA [auth T]IPR045241WD repeat Prp46/PLRG1-likeFamily
WA [auth T]IPR001680WD40 repeatRepeat
WA [auth T]IPR020472G-protein beta WD-40 repeatRepeat
WA [auth T]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
IPR041094Brr2, N-terminal helicase PWI domainDomain
IPR004179Sec63 domainDomain
IPR014756Immunoglobulin E-setHomologous Superfamily
IPR011545DEAD/DEAH box helicase domainDomain
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IPR001650Helicase, C-terminal domain-likeDomain
IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
IPR035892C2 domain superfamilyHomologous Superfamily
XA [auth U]IPR047490Serine/arginine repetitive matrix protein 2, cwf21 domainDomain
XA [auth U]IPR013170mRNA splicing factor Cwf21 domainDomain
XA [auth U]IPR024945Spt5 C-terminal domainDomain
YA [auth V]IPR016024Armadillo-type foldHomologous Superfamily
YA [auth V]IPR003891Initiation factor eIF-4 gamma, MA3Domain
YA [auth V]IPR003890MIF4G-like, type 3Domain
ZA [auth W]IPR019775WD40 repeat, conserved siteConserved Site
ZA [auth W]IPR032847Pre-mRNA-processing factor 17Family
ZA [auth W]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
ZA [auth W]IPR001680WD40 repeatRepeat
ZA [auth W]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
AB [auth X]IPR008984SMAD/FHA domain superfamilyHomologous Superfamily
AB [auth X]IPR000253Forkhead-associated (FHA) domainDomain
BB [auth Y]IPR000504RNA recognition motif domainDomain
BB [auth Y]IPR045844Ist3-like, RNA recognition motifDomain
BB [auth Y]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
BB [auth Y]IPR035979RNA-binding domain superfamilyHomologous Superfamily
CB [auth Z]IPR018609Bud13Family
DB [auth x]IPR011709DEAD-box helicase, OB foldDomain
DB [auth x]IPR001650Helicase, C-terminal domain-likeDomain
DB [auth x]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
DB [auth x]IPR048333Helicase associated domain (HA2), winged-helix domainDomain
DB [auth x]IPR002464DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved siteConserved Site
DB [auth x]IPR007502Helicase-associated domainDomain
DB [auth x]IPR011545DEAD/DEAH box helicase domainDomain
DB [auth x]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
EB [auth y]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
EB [auth y]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
EB [auth y]IPR034168Peptidyl-prolyl cis-trans isomerase E, RNA recognition motifDomain
EB [auth y]IPR016304Peptidyl-prolyl cis-trans isomerase EFamily
EB [auth y]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
EB [auth y]IPR000504RNA recognition motif domainDomain
EB [auth y]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
EB [auth y]IPR035979RNA-binding domain superfamilyHomologous Superfamily
IPR019775WD40 repeat, conserved siteConserved Site
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
IPR001680WD40 repeatRepeat
IPR020472G-protein beta WD-40 repeatRepeat
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
F [auth a],
P [auth h]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
F [auth a],
P [auth h]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
F [auth a],
P [auth h]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
F [auth a],
P [auth h]
IPR047575Sm domainDomain
F [auth a],
P [auth h]
IPR010920LSM domain superfamilyHomologous Superfamily
G [auth b],
Q [auth i]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
G [auth b],
Q [auth i]
IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
G [auth b],
Q [auth i]
IPR047575Sm domainDomain
G [auth b],
Q [auth i]
IPR010920LSM domain superfamilyHomologous Superfamily
H [auth c],
R [auth j]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
H [auth c],
R [auth j]
IPR034102Small nuclear ribonucleoprotein D1Domain
H [auth c],
R [auth j]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
H [auth c],
R [auth j]
IPR047575Sm domainDomain
H [auth c],
R [auth j]
IPR010920LSM domain superfamilyHomologous Superfamily
I [auth d],
S [auth k]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
I [auth d],
S [auth k]
IPR047575Sm domainDomain
I [auth d],
S [auth k]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
I [auth d],
S [auth k]
IPR010920LSM domain superfamilyHomologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ6P2Q9
J [auth f],
T [auth m]
PharosP62306
K [auth e],
U [auth l]
PharosP62304
L [auth g],
V [auth n]
PharosP62308
X [auth p]PharosP08579
Y [auth w]PharosQ12874
Z [auth u]PharosQ15459
AA [auth v]PharosQ15428
BA [auth 1]PharosO75533
CA [auth 2]PharosQ13435
DA [auth 3]PharosQ15393
EA [auth 4]PharosQ15427
FA [auth 5]PharosQ9Y3B4
GA [auth 6]PharosQ7RTV0
HA [auth 7]PharosQ9BWJ5
IA [auth J]PharosQ9BZJ0
JA [auth L]PharosQ99459
PharosQ15029
KA [auth q],
LA [auth r],
MA [auth s],
NA [auth t]
PharosQ9UMS4
OA [auth K]PharosO75934
PA [auth I]PharosQ9HCS7
QA [auth Q]PharosO60306
RA [auth N]PharosP41223
SA [auth O]PharosQ9NW64
TA [auth P]PharosQ9P013
VA [auth S]PharosQ9Y3C6
WA [auth T]PharosO43660
PharosO75643
XA [auth U]PharosQ9UQ35
YA [auth V]PharosQ9HCG8
ZA [auth W]PharosO60508
AB [auth X]PharosQ8TAD8
CB [auth Z]PharosQ9BRD0
DB [auth x]PharosO60231
EB [auth y]PharosQ9UNP9
PharosQ96DI7
F [auth a],
P [auth h]
PharosP62318
G [auth b],
Q [auth i]
PharosP14678
H [auth c],
R [auth j]
PharosP62314
I [auth d],
S [auth k]
PharosP62316