6AHD

The Cryo-EM Structure of Human Pre-catalytic Spliceosome (B complex) at 3.8 angstrom resolution


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyRibonuclease H-like8041105 3000143 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyJAB1/MPN domain-like8053277 3001105 SCOP2B (2022-06-29)
J [auth L]SCOP2B SuperfamilyNop domain8033305 3001551 SCOP2B (2022-06-29)
BB [auth V]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
EA [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
N [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
O [auth c]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
FA [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
VA [auth P]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
R [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
IA [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
YA [auth S]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
CA [auth h]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
S [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
ZA [auth T]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
V [auth W]SCOP2B SuperfamilyCyclophilin-like8042789 3000168 SCOP2B (2022-06-29)
W [auth A0]SCOP2B SuperfamilyUbiquitin-like8038047 3000157 SCOP2B (2022-06-29)
Y [auth Z]SCOP2B SuperfamilyPRP38-like8055808 3002318 SCOP2B (2022-06-29)
JA [auth o]SCOP2B SuperfamilyL domain-like8043993 3001010 SCOP2B (2022-06-29)
KA [auth p]SCOP2B SuperfamilyRNA-binding domain RBD8035327 3000110 SCOP2B (2022-06-29)
PA [auth r]SCOP2B SuperfamilySm-like ribonucleoproteins8063456 3000419 SCOP2B (2022-06-29)
QA [auth s]SCOP2B SuperfamilySm-like ribonucleoproteins8063488 3000419 SCOP2B (2022-06-29)
RA [auth t]SCOP2B SuperfamilySm-like ribonucleoproteins8063472 3000419 SCOP2B (2022-06-29)
SA [auth x]SCOP2B SuperfamilySm-like ribonucleoproteins8063442 3000419 SCOP2B (2022-06-29)
TA [auth y]SCOP2B SuperfamilySm-like ribonucleoproteins8063466 3000419 SCOP2B (2022-06-29)
UA [auth z]SCOP2B SuperfamilySm-like ribonucleoproteins8063492 3000419 SCOP2B (2022-06-29)
EB [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
EB [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052535 3001694 SCOP2B (2022-06-29)
EB [auth 3]SCOP2B SuperfamilyWD40 repeat-like8051197 3001694 SCOP2B (2022-06-29)
EB [auth 3]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
FB [auth 5]SCOP2B SuperfamilyRNA-binding domain RBD8040695 3000110 SCOP2B (2022-06-29)
GB [auth 6]SCOP2B SuperfamilyTriquetra zinc finger motif8051848 3002040 SCOP2B (2022-06-29)
JB [auth 4]SCOP2B SuperfamilyRNA-binding domain RBD8090834 3000110 SCOP2B (2022-06-29)
KB [auth D]SCOP2B SuperfamilyBrl domain-like8036193 3000115 SCOP2B (2022-06-29)
KB [auth D]SCOP2B SuperfamilyE set domains8055093 3000070 SCOP2B (2022-06-29)
F [auth O]SCOP2B SuperfamilyThioredoxin-like8044390 3000031 SCOP2B (2022-06-29)
I [auth M]SCOP2B SuperfamilyL30e-like8043738 3001739 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF10596,PF10597e6ahdA6 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)
APF08082,PF08083e6ahdA3 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)
APF10598e6ahdA5 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)
APF01398,PF08084e6ahdA2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398,PF08084ECOD (1.6)
APF10596e6ahdA4 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
APF12134e6ahdA1 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
J [auth L]PF01798e6ahdL2 A: alpha arraysX: HhH/H2THH: SAM/DNA-glycosylaseT: Nop C-terminal domainF: PF01798ECOD (1.6)
J [auth L]PF01798e6ahdL1 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)
J [auth L]PF09785e6ahdL3 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)
L [auth J]PF06544e6ahdJ1 A: a+b two layersX: Alpha-beta plaitsH: Acylphosphatase-like (From Topology)T: Acylphosphatase-likeF: PF06544ECOD (1.6)
L [auth J]PF08572e6ahdJ2 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)
AB [auth U]PF01423e6ahdU1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
DA [auth i]PF01423e6ahdi1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
M [auth a]PF01423e6ahda1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BB [auth V]PF01423e6ahdV1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
EA [auth j]PF01423e6ahdj1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
N [auth b]PF01423e6ahdb1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
O [auth c]PF01423e6ahdc1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
FA [auth k]PF01423e6ahdk1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
VA [auth P]PF01423e6ahdP1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
P [auth d]PF01423e6ahdd1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
GA [auth l]PF01423e6ahdl1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
WA [auth Q]PF01423e6ahdQ1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
HA [auth m]PF01423e6ahdm1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Q [auth e]PF01423e6ahde1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
XA [auth R]PF01423e6ahdR1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
R [auth f]PF01423e6ahdf1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
IA [auth n]PF01423e6ahdn1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
YA [auth S]PF01423e6ahdS1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
CA [auth h]PF01423e6ahdh1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
S [auth g]PF01423e6ahdg1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
ZA [auth T]PF01423e6ahdT1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
T [auth E]PF00400e6ahdE1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
U [auth X]PF06220e6ahdX1 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF06220ECOD (1.6)
V [auth W]PF00160e6ahdW1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: PF00160ECOD (1.6)
W [auth A0]PF00240e6ahdA01 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: PF00240ECOD (1.6)
Y [auth Z]PF03371e6ahdZ1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Pre-mRNA-splicing factor 38A (From Topology)T: Pre-mRNA-splicing factor 38AF: PF03371ECOD (1.6)
Z [auth 8]PF12171e6ahd81 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF12171ECOD (1.6)
AA [auth Y]PF00400e6ahdY1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
AA [auth Y]PF08513e6ahdY2 A: alpha duplicates or obligate multimersX: Lis-homology dimerization domain (From Topology)H: Lis-homology dimerization domain (From Topology)T: Lis-homology dimerization domainF: PF08513ECOD (1.6)
JA [auth o]PF14580e6ahdo1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Leucine-rich repeats (From Topology)T: Leucine-rich repeatsF: PF14580ECOD (1.6)
KA [auth p]PF00076e6ahdp1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
LA [auth u]PF01805,PF12230e6ahdu1 A: alpha bundlesX: Surp module (SWAP domain) (From Topology)H: Surp module (SWAP domain) (From Topology)T: Surp module (SWAP domain)F: PF01805,PF12230ECOD (1.6)
MA [auth v]PF16835e6ahdv1 A: beta sandwichesX: HSP20-likeH: Pre-mRNA-splicing factor PRP11 C-terminal domain (From Topology)T: Pre-mRNA-splicing factor PRP11 C-terminal domainF: PF16835ECOD (1.6)
OA [auth q]PF01423e6ahdq1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
PA [auth r]PF01423e6ahdr1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
QA [auth s]PF01423e6ahds1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
RA [auth t]PF01423e6ahdt1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
SA [auth x]PF01423e6ahdx1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
TA [auth y]PF01423e6ahdy1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
UA [auth z]PF01423e6ahdz1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
EB [auth 3]PF03178,PF10433e6ahd34 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF03178,PF10433ECOD (1.6)
EB [auth 3]PF10433e6ahd33 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF10433ECOD (1.6)
EB [auth 3]PF03178e6ahd31 A: alpha arraysX: HTHH: HTHT: tri-helicalF: PF03178ECOD (1.6)
FB [auth 5]PF00076e6ahd51 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
GB [auth 6]PF03660e6ahd61 A: few secondary structure elementsX: Glucocorticoid receptor-likeH: LIM domain-likeT: PHD finger-like domain-containing protein 5AF: PF03660ECOD (1.6)
HB [auth 7]PF07189e6ahd71 A: alpha arraysX: RDS3 complex subunit 10 (From Topology)H: RDS3 complex subunit 10 (From Topology)T: RDS3 complex subunit 10F: PF07189ECOD (1.6)
JB [auth 4]PF00076e6ahd41 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
KB [auth D]PF02889e6ahdD3 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: PF02889ECOD (1.6)
KB [auth D]F_UNCLASSIFIEDe6ahdD5 A: alpha arraysX: HTHH: HTHT: wingedF: F_UNCLASSIFIEDECOD (1.6)
KB [auth D]F_UNCLASSIFIEDe6ahdD1 A: alpha arraysX: HhH/H2THH: SAM-like subdomain in Sec63-like proteins (From Topology)T: SAM-like subdomain in Sec63-like proteinsF: F_UNCLASSIFIEDECOD (1.6)
KB [auth D]PF02889e6ahdD12 A: alpha arraysX: Sec63 N-terminal subdomain-like (From Topology)H: Sec63 N-terminal subdomain-like (From Topology)T: Sec63 N-terminal subdomain-likeF: PF02889ECOD (1.6)
KB [auth D]PF00270e6ahdD11 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00270ECOD (1.6)
KB [auth D]PF00271e6ahdD2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00271ECOD (1.6)
F [auth O]PF02966e6ahdO1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PF02966ECOD (1.6)
G [auth C]PF03144e6ahdC2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF03144ECOD (1.6)
G [auth C]PF03764e6ahdC5 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)
G [auth C]PF00679e6ahdC1 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)
G [auth C]PF14492e6ahdC4 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)
G [auth C]PF00009e6ahdC3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00009ECOD (1.6)
I [auth M]PF01248e6ahdM1 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
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
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
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 L]PF09785Prp31 C terminal domain (Prp31_C)Prp31 C terminal domain- Family
J [auth L]PF01798snoRNA binding domain, fibrillarin (Nop)snoRNA binding domain, fibrillarin- Family
K [auth 9]PF03343SART-1 family (SART-1)SART-1 family- Family
L [auth J]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
L [auth J]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
BB [auth V],
EA [auth j],
N [auth b]
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 k],
O [auth c],
VA [auth P]
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 n],
R [auth f],
YA [auth S]
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
CA [auth h],
S [auth g],
ZA [auth T]
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
T [auth E]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
U [auth X]PF06220U1 zinc finger (zf-U1)U1 zinc fingerThis family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class o ...This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class of weak 5' ss is promoted by binding of the protein TIA-1 to uridine-rich sequences immediately downstream from the 5' ss. Binding of TIA-1 in the vicinity of a 5' ss helps to stabilise U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator [1]. This domain is probably a zinc-binding. It is found in multiple copies in some members of the family.
Domain
V [auth W]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
W [auth A0]PF00240Ubiquitin family (ubiquitin)Ubiquitin familyThis family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry ...This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].
Domain
X [auth 0]PF06991Microfibril-associated/Pre-mRNA processing (MFAP1)Microfibril-associated/Pre-mRNA processing- Family
Y [auth Z]PF03371PRP38 family (PRP38)PRP38 family- Family
Z [auth 8]PF12171Zinc-finger double-stranded RNA-binding (zf-C2H2_jaz)Zinc-finger double-stranded RNA-binding- Family
AA [auth Y]PF17814LisH-like dimerisation domain (LisH_TPL)LisH-like dimerisation domainTOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif [1].Domain
AA [auth Y]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
JA [auth o]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
KA [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
LA [auth u]PF01805Surp module (Surp)Surp module- Family
MA [auth v]PF16835Pre-mRNA-splicing factor SF3a complex subunit 2 (Prp11) (SF3A2)Pre-mRNA-splicing factor SF3a complex subunit 2 (Prp11)SF3A2 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 ...SF3A2 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). with Prp21 wrapping around Prp11 [1].
Domain
NA [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
NA [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
OA [auth q]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
PA [auth r]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
QA [auth s]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
RA [auth t]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
SA [auth x]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
TA [auth y]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
UA [auth z]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
CB [auth K]PF08799pre-mRNA processing factor 4 (PRP4) like (PRP4)pre-mRNA processing factor 4 (PRP4) likeThis small domain is found on PRP4 ribonuleoproteins. PRP4 is a U4/U6 small nuclear ribonucleoprotein that is involved in pre-mRNA processing.Domain
CB [auth K]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
EB [auth 3]PF10433Mono-functional DNA-alkylating methyl methanesulfonate N-term (MMS1_N)Mono-functional DNA-alkylating methyl methanesulfonate N-term- Repeat
EB [auth 3]PF03178CPSF A subunit region (CPSF_A)CPSF A subunit region- Repeat
FB [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
GB [auth 6]PF03660PHF5-like protein (PHF5)PHF5-like protein- Family
HB [auth 7]PF07189Splicing factor 3B subunit 10 (SF3b10) (SF3b10)Splicing factor 3B subunit 10 (SF3b10)- Family
IB [auth 2]PF04037Domain of unknown function (DUF382) (DUF382)Domain of unknown function (DUF382)- Family
IB [auth 2]PF04046PSP (PSP)PSP- Family
JB [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
KB [auth D]PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
KB [auth D]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
KB [auth D]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
F [auth O]PF02966Mitosis protein DIM1 (DIM1)Mitosis protein DIM1- Domain
G [auth C]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
G [auth C]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
G [auth C]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
G [auth C]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
G [auth C]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
H [auth N]PF14559Tetratricopeptide repeat (TPR_19)Tetratricopeptide repeat- Repeat
H [auth N]PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
H [auth N]PF06424PRP1 splicing factor, N-terminal (PRP1_N)PRP1 splicing factor, N-terminalThis domain is specific to the N-terminal part of the prp1 splicing factor, which is involved in mRNA splicing (and possibly also poly(A)+ RNA nuclear export and cell cycle progression). This domain is specific to the N terminus of the RNA splicing f ...This domain is specific to the N-terminal part of the prp1 splicing factor, which is involved in mRNA splicing (and possibly also poly(A)+ RNA nuclear export and cell cycle progression). This domain is specific to the N terminus of the RNA splicing factor encoded by prp1 [1]. It is involved in mRNA splicing and possibly also poly(A)and RNA nuclear export and cell cycle progression.
Domain
I [auth M]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
Pre-mRNA-processing-splicing factor 8
J [auth L]U4/U6 small nuclear ribonucleoprotein Prp31
K [auth 9]U4/U6.U5 tri-snRNP-associated protein 1
L [auth J]U4/U6 small nuclear ribonucleoprotein Prp3
AB [auth U],
DA [auth i],
M [auth a]
SmB---
BB [auth V],
EA [auth j],
N [auth b]
Small nuclear ribonucleoprotein Sm D1
FA [auth k],
O [auth c],
VA [auth P]
Small nuclear ribonucleoprotein Sm D2
GA [auth l],
P [auth d],
WA [auth Q]
SmE---
HA [auth m],
Q [auth e],
XA [auth R]
SmF---
IA [auth n],
R [auth f],
YA [auth S]
Small nuclear ribonucleoprotein G
CA [auth h],
S [auth g],
ZA [auth T]
Small nuclear ribonucleoprotein Sm D3
B [auth I]U4snRNA---
T [auth E]U5 small nuclear ribonucleoprotein 40 kDa protein
U [auth X]WW domain-binding protein 4
V [auth W]Peptidyl-prolyl cis-trans isomerase H
W [auth A0]Ubiquitin-like protein 5
X [auth 0]Microfibrillar-associated protein 1
Y [auth Z]Pre-mRNA-splicing factor 38A
Z [auth 8]Zinc finger matrin-type protein 2
AA [auth Y]WD40 repeat-containing protein SMU1-
BA [auth H]U2snRNA---
JA [auth o]U2 small nuclear ribonucleoprotein A'
C [auth B]U5snRNA---
KA [auth p]U2 small nuclear ribonucleoprotein B''
LA [auth u]Splicing factor 3A subunit 1
MA [auth v]Splicing factor 3A subunit 2
NA [auth w]Splicing factor 3A subunit 3
OA [auth q]U6 snRNA-associated Sm-like protein LSm2
PA [auth r]U6 snRNA-associated Sm-like protein LSm3
QA [auth s]U6 snRNA-associated Sm-like protein LSm4
RA [auth t]U6 snRNA-associated Sm-like protein LSm5
SA [auth x]U6 snRNA-associated Sm-like protein LSm6
TA [auth y]U6 snRNA-associated Sm-like protein LSm7
D [auth F]U6snRNA---
UA [auth z]U6 snRNA-associated Sm-like protein LSm8
CB [auth K]U4/U6 small nuclear ribonucleoprotein Prp4
DB [auth 1]Splicing factor 3B subunit 1
EB [auth 3]Splicing factor 3B subunit 3
FB [auth 5]SF3b14a, Splicing factor 3B subunit 6
GB [auth 6]PHD finger-like domain-containing protein 5A
HB [auth 7]SF3b5, Splicing factor 3B subunit 5
IB [auth 2]SF3b145, Splicing factor 3B subunit 2
JB [auth 4]SF3b49, Splicing factor 3B subunit 4
KB [auth D]Brr2, U5 small nuclear ribonucleoprotein 200 kDa helicase
E [auth G]pre-mRNA---
F [auth O]Thioredoxin-like protein 4A-
G [auth C]116 kDa U5 small nuclear ribonucleoprotein component
H [auth N]Pre-mRNA-processing factor 6
I [auth M]NHP2-like protein 1

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 L]IPR042239Nop, C-terminal domainHomologous Superfamily
J [auth L]IPR019175Prp31 C-terminalDomain
J [auth L]IPR002687Nop domainDomain
J [auth L]IPR012976NOSICDomain
J [auth L]IPR027105U4/U6 small nuclear ribonucleoprotein Prp31Family
J [auth L]IPR036070Nop domain superfamilyHomologous Superfamily
K [auth 9]IPR045347HIND motifConserved Site
K [auth 9]IPR005011SNU66/SART1 familyFamily
L [auth J]IPR027104U4/U6 small nuclear ribonucleoprotein Prp3Family
L [auth J]IPR002483PWI domainDomain
L [auth J]IPR013881Pre-mRNA-splicing factor 3 domainDomain
L [auth J]IPR036483PWI domain superfamilyHomologous Superfamily
L [auth J]IPR010541Small nuclear ribonucleoprotein Prp3, C-terminal domainDomain
BB [auth V],
EA [auth j],
N [auth b]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
BB [auth V],
EA [auth j],
N [auth b]
IPR034102Small nuclear ribonucleoprotein D1Domain
BB [auth V],
EA [auth j],
N [auth b]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
BB [auth V],
EA [auth j],
N [auth b]
IPR047575Sm domainDomain
BB [auth V],
EA [auth j],
N [auth b]
IPR010920LSM domain superfamilyHomologous Superfamily
FA [auth k],
O [auth c],
VA [auth P]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
FA [auth k],
O [auth c],
VA [auth P]
IPR047575Sm domainDomain
FA [auth k],
O [auth c],
VA [auth P]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
FA [auth k],
O [auth c],
VA [auth P]
IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth n],
R [auth f],
YA [auth S]
IPR044641Sm-like protein Lsm7/SmGFamily
IA [auth n],
R [auth f],
YA [auth S]
IPR034098Small nuclear ribonucleoprotein GFamily
IA [auth n],
R [auth f],
YA [auth S]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
IA [auth n],
R [auth f],
YA [auth S]
IPR047575Sm domainDomain
IA [auth n],
R [auth f],
YA [auth S]
IPR010920LSM domain superfamilyHomologous Superfamily
CA [auth h],
S [auth g],
ZA [auth T]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
CA [auth h],
S [auth g],
ZA [auth T]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
CA [auth h],
S [auth g],
ZA [auth T]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
CA [auth h],
S [auth g],
ZA [auth T]
IPR047575Sm domainDomain
CA [auth h],
S [auth g],
ZA [auth T]
IPR010920LSM domain superfamilyHomologous Superfamily
T [auth E]IPR019775WD40 repeat, conserved siteConserved Site
T [auth E]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
T [auth E]IPR001680WD40 repeatRepeat
T [auth E]IPR020472G-protein beta WD-40 repeatRepeat
T [auth E]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
U [auth X]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
U [auth X]IPR040023WW domain-binding protein 4Family
U [auth X]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
U [auth X]IPR036020WW domain superfamilyHomologous Superfamily
U [auth X]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
U [auth X]IPR001202WW domainDomain
U [auth X]IPR013085U1-C, C2H2-type zinc fingerDomain
V [auth W]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
V [auth W]IPR024936Cyclophilin-type peptidyl-prolyl cis-trans isomeraseFamily
V [auth W]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
V [auth W]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
W [auth A0]IPR039732Ubiquitin-like modifier Hub1/Ubl5Family
W [auth A0]IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
W [auth A0]IPR000626Ubiquitin-like domainDomain
X [auth 0]IPR033194Microfibrillar-associated protein 1Family
X [auth 0]IPR009730Micro-fibrillar-associated protein 1, C-terminalDomain
Y [auth Z]IPR024767Pre-mRNA-splicing factor 38, C-terminalDomain
Y [auth Z]IPR005037Pre-mRNA-splicing factor 38Family
Z [auth 8]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
Z [auth 8]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
Z [auth 8]IPR040107U4/U6.U5 small nuclear ribonucleoprotein component Snu23Family
Z [auth 8]IPR022755Zinc finger, double-stranded RNA bindingDomain
AA [auth Y]IPR019775WD40 repeat, conserved siteConserved Site
AA [auth Y]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
AA [auth Y]IPR006595CTLH, C-terminal LisH motifDomain
AA [auth Y]IPR045184WD40 repeat-containing protein SMU1Family
AA [auth Y]IPR001680WD40 repeatRepeat
AA [auth Y]IPR020472G-protein beta WD-40 repeatRepeat
AA [auth Y]IPR006594LIS1 homology motifConserved Site
AA [auth Y]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
JA [auth o]IPR001611Leucine-rich repeatRepeat
JA [auth o]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
JA [auth o]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
KA [auth p]IPR034562U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2Domain
KA [auth p]IPR000504RNA recognition motif domainDomain
KA [auth p]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
KA [auth p]IPR035979RNA-binding domain superfamilyHomologous Superfamily
KA [auth p]IPR034564U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1Domain
LA [auth u]IPR045146Splicing factor 3A subunit 1Family
LA [auth u]IPR035967SWAP/Surp superfamilyHomologous Superfamily
LA [auth u]IPR000061SWAP/SurpDomain
LA [auth u]IPR000626Ubiquitin-like domainDomain
LA [auth u]IPR035563Splicing factor 3A subunit 1, ubiquitin domainDomain
LA [auth u]IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
LA [auth u]IPR022030Splicing factor 3A subunit 1, conserved domainDomain
MA [auth v]IPR031781SF3A2 domainDomain
MA [auth v]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
MA [auth v]IPR013087Zinc finger C2H2-typeDomain
MA [auth v]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
MA [auth v]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
NA [auth w]IPR021966Splicing factor SF3a60 binding domainDomain
NA [auth w]IPR031774SF3A3 domainDomain
NA [auth w]IPR024598Splicing factor SF3a60 /Prp9 subunit, C-terminalDomain
NA [auth w]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
NA [auth w]IPR025086SDE2-like, C-terminal domainDomain
OA [auth q]IPR001163Sm domain, eukaryotic/archaea-typeDomain
OA [auth q]IPR047575Sm domainDomain
OA [auth q]IPR010920LSM domain superfamilyHomologous Superfamily
OA [auth q]IPR016654U6 snRNA-associated Sm-like protein LSm2Family
PA [auth r]IPR040002U6 snRNA-associated Sm-like protein Lsm3Family
PA [auth r]IPR001163Sm domain, eukaryotic/archaea-typeDomain
PA [auth r]IPR047575Sm domainDomain
PA [auth r]IPR010920LSM domain superfamilyHomologous Superfamily
PA [auth r]IPR034105Sm-like protein Lsm3Domain
QA [auth s]IPR001163Sm domain, eukaryotic/archaea-typeDomain
QA [auth s]IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
QA [auth s]IPR047575Sm domainDomain
QA [auth s]IPR034101Sm-like protein Lsm4Domain
QA [auth s]IPR010920LSM domain superfamilyHomologous Superfamily
RA [auth t]IPR001163Sm domain, eukaryotic/archaea-typeDomain
RA [auth t]IPR047575Sm domainDomain
RA [auth t]IPR033871Sm-like protein LSm5Domain
RA [auth t]IPR010920LSM domain superfamilyHomologous Superfamily
SA [auth x]IPR001163Sm domain, eukaryotic/archaea-typeDomain
SA [auth x]IPR047575Sm domainDomain
SA [auth x]IPR016487Sm-like protein Lsm6/SmFFamily
SA [auth x]IPR010920LSM domain superfamilyHomologous Superfamily
TA [auth y]IPR001163Sm domain, eukaryotic/archaea-typeDomain
TA [auth y]IPR047575Sm domainDomain
TA [auth y]IPR044641Sm-like protein Lsm7/SmGFamily
TA [auth y]IPR010920LSM domain superfamilyHomologous Superfamily
TA [auth y]IPR017132Sm-like protein Lsm7Family
UA [auth z]IPR001163Sm domain, eukaryotic/archaea-typeDomain
UA [auth z]IPR047575Sm domainDomain
UA [auth z]IPR034103Sm-like protein Lsm8Domain
UA [auth z]IPR010920LSM domain superfamilyHomologous Superfamily
UA [auth z]IPR044642U6 snRNA-associated Sm-like protein Lsm1/8Family
CB [auth K]IPR019775WD40 repeat, conserved siteConserved Site
CB [auth K]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
CB [auth K]IPR036285PRP4-like superfamilyHomologous Superfamily
CB [auth K]IPR014906Pre-mRNA processing factor 4 (PRP4)-likeDomain
CB [auth K]IPR001680WD40 repeatRepeat
CB [auth K]IPR020472G-protein beta WD-40 repeatRepeat
CB [auth K]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
DB [auth 1]IPR016024Armadillo-type foldHomologous Superfamily
DB [auth 1]IPR011989Armadillo-like helicalHomologous Superfamily
DB [auth 1]IPR015016Splicing factor 3B subunit 1Domain
DB [auth 1]IPR038737Splicing factor 3B subunit 1-likeFamily
EB [auth 3]IPR018846Cleavage/polyadenylation specificity factor, A subunit, N-terminalDomain
EB [auth 3]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
EB [auth 3]IPR004871Cleavage/polyadenylation specificity factor, A subunit, C-terminalDomain
EB [auth 3]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
FB [auth 5]IPR000504RNA recognition motif domainDomain
FB [auth 5]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
FB [auth 5]IPR034150SF3B6, RNA recognition motifDomain
FB [auth 5]IPR035979RNA-binding domain superfamilyHomologous Superfamily
GB [auth 6]IPR005345PHF5-likeFamily
HB [auth 7]IPR017089Splicing factor 3B, subunit 5Family
HB [auth 7]IPR009846Splicing factor 3B subunit 5/RDS3 complex subunit 10Family
IB [auth 2]IPR006568PSP, proline-richDomain
IB [auth 2]IPR007180Domain of unknown function DUF382Domain
IB [auth 2]IPR003034SAP domainDomain
JB [auth 4]IPR034159SF3B4, RNA recognition motif 2Domain
JB [auth 4]IPR000504RNA recognition motif domainDomain
JB [auth 4]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
JB [auth 4]IPR035979RNA-binding domain superfamilyHomologous Superfamily
JB [auth 4]IPR034158SF3B4, RNA recognition motif 1Domain
KB [auth D]IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
KB [auth D]IPR041094Brr2, N-terminal helicase PWI domainDomain
KB [auth D]IPR004179Sec63 domainDomain
KB [auth D]IPR014756Immunoglobulin E-setHomologous Superfamily
KB [auth D]IPR011545DEAD/DEAH box helicase domainDomain
KB [auth D]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
KB [auth D]IPR001650Helicase, C-terminal domain-likeDomain
KB [auth D]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
KB [auth D]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
KB [auth D]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
KB [auth D]IPR035892C2 domain superfamilyHomologous Superfamily
F [auth O]IPR004123Dim1 familyFamily
F [auth O]IPR036249Thioredoxin-like superfamilyHomologous Superfamily
G [auth C]IPR005517Translation elongation factor EFG/EF2, domain IVDomain
G [auth C]IPR000795Translational (tr)-type GTP-binding domainDomain
G [auth C]IPR035647EF-G domain III/V-likeHomologous Superfamily
G [auth C]IPR035655116kDa U5 small nuclear ribonucleoprotein component, C-terminalDomain
G [auth C]IPR041095Elongation Factor G, domain IIDomain
G [auth C]IPR004161Translation elongation factor EFTu-like, domain 2Domain
G [auth C]IPR009000Translation protein, beta-barrel domain superfamilyHomologous Superfamily
G [auth C]IPR020568Ribosomal protein uS5 domain 2-type superfamilyHomologous Superfamily
G [auth C]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
G [auth C]IPR014721Small ribosomal subunit protein uS5 domain 2-type fold, subgroupHomologous Superfamily
G [auth C]IPR031950116kDa U5 small nuclear ribonucleoprotein component, N-terminalDomain
G [auth C]IPR000640Elongation factor EFG, domain V-likeDomain
G [auth C]IPR044121Snu114, GTP-binding domainDomain
G [auth C]IPR005225Small GTP-binding protein domainDomain
H [auth N]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
H [auth N]IPR010491PRP1 splicing factor, N-terminalDomain
H [auth N]IPR003107HAT (Half-A-TPR) repeatRepeat
H [auth N]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
H [auth N]IPR019734Tetratricopeptide repeatRepeat
I [auth M]IPR002415H/ACA ribonucleoprotein complex, subunit Nhp2-likeFamily
I [auth M]IPR029064Ribosomal protein eL30-like superfamilyHomologous Superfamily
I [auth M]IPR018492Ribosomal protein eL8/Nhp2 familyFamily
I [auth M]IPR004038Ribosomal protein eL8/eL30/eS12/Gadd45Domain
I [auth M]IPR004037Large ribosomal subunit protein eL8-like, conserved siteConserved Site

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ6P2Q9
J [auth L]PharosQ8WWY3
K [auth 9]PharosO43290
L [auth J]PharosO43395
BB [auth V],
EA [auth j],
N [auth b]
PharosP62314
FA [auth k],
O [auth c],
VA [auth P]
PharosP62316
IA [auth n],
R [auth f],
YA [auth S]
PharosP62308
CA [auth h],
S [auth g],
ZA [auth T]
PharosP62318
T [auth E]PharosQ96DI7
U [auth X]PharosO75554
V [auth W]PharosO43447
W [auth A0]PharosQ9BZL1
X [auth 0]PharosP55081
Y [auth Z]PharosQ8NAV1
Z [auth 8]PharosQ96NC0
AA [auth Y]PharosQ2TAY7
KA [auth p]PharosP08579
LA [auth u]PharosQ15459
MA [auth v]PharosQ15428
NA [auth w]PharosQ12874
OA [auth q]PharosQ9Y333
PA [auth r]PharosP62310
QA [auth s]PharosQ9Y4Z0
RA [auth t]PharosQ9Y4Y9
SA [auth x]PharosP62312
TA [auth y]PharosQ9UK45
UA [auth z]PharosO95777
CB [auth K]PharosO43172
DB [auth 1]PharosO75533
EB [auth 3]PharosQ15393
FB [auth 5]PharosQ9Y3B4
GB [auth 6]PharosQ7RTV0
HB [auth 7]PharosQ9BWJ5
IB [auth 2]PharosQ13435
JB [auth 4]PharosQ15427
KB [auth D]PharosO75643
F [auth O]PharosP83876
G [auth C]PharosQ15029
H [auth N]PharosO94906
I [auth M]PharosP55769