6ID0

Cryo-EM structure of a human intron lariat spliceosome prior to Prp43 loaded (ILS1 complex) at 2.9 angstrom resolution

External Resource: Annotation


Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Cd6id0c2 All beta proteins Reductase/isomerase/elongation factor common domain Translation proteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd6id0c1 Alpha and beta proteins (a/b) P-loop containing nucleoside triphosphate hydrolases P-loop containing nucleoside triphosphate hydrolases automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd6id0c4 Alpha and beta proteins (a+b) Ribosomal protein S5 domain 2-like Ribosomal protein S5 domain 2-like automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd6id0c3 Alpha and beta proteins (a+b) Ferredoxin-like EF-G C-terminal domain-like automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
D [auth E]d6id0e_ All beta proteins 7-bladed beta-propeller WD40 repeat-like automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
I [auth N]d6id0n_ Small proteins Pre-mRNA splicing factor Cwf14-like Pre-mRNA splicing factor Cwf14-like Pre-mRNA splicing factor Cwf14-like automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
M [auth S]d6id0s_ All beta proteins Cyclophilin-like Cyclophilin-like Cyclophilin (peptidylprolyl isomerase) Peptidyl-prolyl cis-trans isomerase-like 1, PPIL1 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
N [auth T]d6id0t_ All beta proteins 7-bladed beta-propeller WD40 repeat-like automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
FA [auth h]d6id0h_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
T [auth a]d6id0a_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
GA [auth i]d6id0i_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
U [auth b]d6id0b_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
HA [auth j]d6id0j_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D1 core SNRNP protein (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
IA [auth k]d6id0k_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D2 core SNRNP protein (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
W [auth d]d6id0d_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D2 core SNRNP protein (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
JA [auth m]d6id0m_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
X [auth f]d6id0f_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
KA [auth l]d6id0l_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Z [auth g]d6id0g_ All beta proteins Sm-like fold Sm-like ribonucleoproteins automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
AA [auth q]d6id0q1 Small proteins RING/U-box RING/U-box automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
AA [auth q]d6id0q2 Coiled coil proteins Parallel coiled-coil Pre-mRNA splicing factor Prp19 coiled coil domain automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
BA [auth r]d6id0r1 Small proteins RING/U-box RING/U-box automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
BA [auth r]d6id0r2 Coiled coil proteins Parallel coiled-coil Pre-mRNA splicing factor Prp19 coiled coil domain automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
MA [auth o]d6id0o_ Alpha and beta proteins (a/b) Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) L domain-like U2A'-like automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
NA [auth p]d6id0p_ Alpha and beta proteins (a+b) Ferredoxin-like RNA-binding domain, RBD, aka RNA recognition motif (RRM) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
PA [auth y]d6id0y_ Alpha and beta proteins (a+b) Ferredoxin-like RNA-binding domain, RBD, aka RNA recognition motif (RRM) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyRibonuclease H-like8041105 3000143 SCOP2B (2022-06-29)
G [auth L]SCOP2B SuperfamilyHomeodomain-like8089608 3000001 SCOP2B (2022-06-29)
J [auth O]SCOP2B SuperfamilyRNA-binding domain RBD8064957 3000110 SCOP2B (2022-06-29)
L [auth R]SCOP2B SuperfamilyPre-mRNA-processing protein 45-like8092740 3002618 SCOP2B (2022-06-29)
M [auth S]SCOP2B SuperfamilyCyclophilin-like8033930 3000168 SCOP2B (2022-06-29)
FA [auth h]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
T [auth a]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
GA [auth i]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
U [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
HA [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
V [auth c]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
IA [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
W [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
JA [auth m]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
X [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
KA [auth l]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
Y [auth e]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
LA [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
Z [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
MA [auth o]SCOP2B SuperfamilyL domain-like8043993 3001010 SCOP2B (2022-06-29)
NA [auth p]SCOP2B SuperfamilyRNA-binding domain RBD8035327 3000110 SCOP2B (2022-06-29)
OA [auth Q]SCOP2B SuperfamilyARM repeat-like8090869 3000116 SCOP2B (2022-06-29)
OA [auth Q]SCOP2B SuperfamilyRecA-like P-loop NTPases8090871 3002019 SCOP2B (2022-06-29)
OA [auth Q]SCOP2B SuperfamilyRecA-like P-loop NTPases8090872 3002019 SCOP2B (2022-06-29)
OA [auth Q]SCOP2B SuperfamilyUpf1 beta-barrel domain-like8090870 3002168 SCOP2B (2022-06-29)
PA [auth y]SCOP2B SuperfamilyRNA-binding domain RBD8039202 3000110 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF10596,PF10597e6id0A5 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,PF08083e6id0A3 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)
APF10598e6id0A4 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)
APF10596e6id0A1 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
APF12134e6id0A2 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
CPF03144e6id0C1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF03144ECOD (1.6)
CPF03764e6id0C5 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)
CPF00679e6id0C4 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)
CPF14492e6id0C3 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)
CPF00009,PF16004e6id0C2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00009,PF16004ECOD (1.6)
D [auth E]PF00400e6id0E1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
F [auth J]PF02184e6id0J1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF02184ECOD (1.6)
I [auth N]PF01125e6id0N1 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: PF01125ECOD (1.6)
J [auth O]PF00076e6id0O1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
J [auth O]PF21369e6id0O2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF21369ECOD (1.6)
J [auth O]F_UNCLASSIFIEDe6id0O3 A: few secondary structure elementsX: CCCH zinc fingerH: CCCH zinc finger (From Topology)T: CCCH zinc fingerF: F_UNCLASSIFIEDECOD (1.6)
M [auth S]PF00160e6id0S1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: PF00160ECOD (1.6)
N [auth T]PF00400e6id0T1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
O [auth W]PF00400e6id0W1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
S [auth I]F_UNCLASSIFIEDe6id0I1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
FA [auth h]PF01423e6id0h1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
T [auth a]PF01423e6id0a1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
GA [auth i]PF01423e6id0i1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
U [auth b]PF01423e6id0b1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
HA [auth j]PF01423e6id0j1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
V [auth c]PF01423e6id0c1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
IA [auth k]PF01423e6id0k1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
W [auth d]PF01423e6id0d1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
JA [auth m]PF01423e6id0m1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
X [auth f]PF01423e6id0f1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
KA [auth l]PF01423e6id0l1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Y [auth e]PF01423e6id0e1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
LA [auth n]PF01423e6id0n1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Z [auth g]PF01423e6id0g1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
MA [auth o]PF14580e6id0o1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Leucine-rich repeats (From Topology)T: Leucine-rich repeatsF: PF14580ECOD (1.6)
NA [auth p]PF00076e6id0p1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
OA [auth Q]PF21143e6id0Q5 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF21143ECOD (1.6)
OA [auth Q]PF16399e6id0Q2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF16399ECOD (1.6)
OA [auth Q]PF21144e6id0Q4 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: PF21144ECOD (1.6)
OA [auth Q]PF13086e6id0Q1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF13086ECOD (1.6)
OA [auth Q]PF13087e6id0Q3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF13087ECOD (1.6)
PA [auth y]PF00076e6id0y1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
D [auth E]2.130.10.10 Mainly Beta 7 Propeller Methylamine Dehydrogenase Chain HCATH (4.3.0)
M [auth S]2.40.100.10 Mainly Beta Beta Barrel Cyclophilin Cyclophilin-likeCATH (4.3.0)
FA [auth h]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
T [auth a]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
HA [auth j]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
V [auth c]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
IA [auth k]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
W [auth d]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
JA [auth m]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
X [auth f]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
KA [auth l]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Y [auth e]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
LA [auth n]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Z [auth g]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
MA [auth o]3.80.10.10 Alpha Beta Alpha-Beta Horseshoe Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) Ribonuclease InhibitorCATH (4.3.0)
NA [auth p]3.30.70.330 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits RRM (RNA recognition motif) domainCATH (4.3.0)
PA [auth y]3.30.70.330 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits RRM (RNA recognition motif) domainCATH (4.3.0)

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
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
PF16004116 kDa U5 small nuclear ribonucleoprotein component N-terminus (EFTUD2)116 kDa U5 small nuclear ribonucleoprotein component N-terminus- Family
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
D [auth E]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
F [auth J]PF02184HAT (Half-A-TPR) repeat (HAT)HAT (Half-A-TPR) repeat- Repeat
G [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
H [auth M]PF08231SYF2 splicing factor (SYF2)SYF2 splicing factorProteins in this family are involved in cell cycle progression and pre-mRNA splicing [1] [2].Domain
I [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
J [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
J [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
K [auth P]PF04889Cwf15/Cwc15 cell cycle control protein (Cwf_Cwc_15)Cwf15/Cwc15 cell cycle control protein- Family
L [auth R]PF02731SKIP/SNW domain (SKIP_SNW)SKIP/SNW domain- Family
M [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
N [auth T]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
O [auth W]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
R [auth U]PF04676Protein similar to CwfJ C-terminus 2 (CwfJ_C_2)Protein similar to CwfJ C-terminus 2- Family
R [auth U]PF04677Protein similar to CwfJ C-terminus 1 (CwfJ_C_1)Protein similar to CwfJ C-terminus 1- Family
S [auth I]PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
FA [auth h],
T [auth a]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
GA [auth i],
U [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
HA [auth j],
V [auth c]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
IA [auth k],
W [auth d]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
JA [auth m],
X [auth f]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
KA [auth l],
Y [auth e]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
LA [auth n],
Z [auth g]		PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
AA [auth q],
BA [auth r],
CA [auth s],
DA [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
AA [auth q],
BA [auth r],
CA [auth s],
DA [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
EA [auth K]PF05700Breast carcinoma amplified sequence 2 (BCAS2) (BCAS2)Breast carcinoma amplified sequence 2 (BCAS2)- Family
MA [auth o]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
NA [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
OA [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
OA [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
OA [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
OA [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
OA [auth Q]PF16399Intron-binding protein aquarius N-terminal (Aquarius_N_1st)Intron-binding protein aquarius N-terminal- Repeat
PA [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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Pre-mRNA-processing-splicing factor 8
U5snRNA---
116 kDa U5 small nuclear ribonucleoprotein component
D [auth E]U5 small nuclear ribonucleoprotein 40 kDa protein
E [auth F]U6snRNA---
F [auth J]Crooked neck-like protein 1
G [auth L]Cell division cycle 5-like protein
H [auth M]Pre-mRNA-splicing factor SYF2
I [auth N]Protein BUD31 homolog
J [auth O]Pre-mRNA-splicing factor RBM22
K [auth P]Spliceosome-associated protein CWC15 homolog
L [auth R]SNW domain-containing protein 1
M [auth S]Peptidyl-prolyl cis-trans isomerase-like 1
N [auth T]Pleiotropic regulator 1-
O [auth W]Pre-mRNA-processing factor 17
P [auth G]pre-mRNA---
Q [auth H]U2snRNA---
R [auth U]CWF19-like protein 2-
S [auth I]Pre-mRNA-splicing factor SYF1-
FA [auth h],
T [auth a]		Small nuclear ribonucleoprotein Sm D3
GA [auth i],
U [auth b]		Small nuclear ribonucleoprotein-associated protein
HA [auth j],
V [auth c]		Small nuclear ribonucleoprotein Sm D1
IA [auth k],
W [auth d]		Small nuclear ribonucleoprotein Sm D2
JA [auth m],
X [auth f]		Small nuclear ribonucleoprotein F
KA [auth l],
Y [auth e]		Small nuclear ribonucleoprotein E
LA [auth n],
Z [auth g]		Small nuclear ribonucleoprotein G
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		Pre-mRNA-processing factor 19
EA [auth K]Pre-mRNA-splicing factor SPF27-
MA [auth o]U2 small nuclear ribonucleoprotein A'
NA [auth p]U2 small nuclear ribonucleoprotein B''
OA [auth Q]RNA helicase aquarius
PA [auth y]Peptidyl-prolyl cis-trans isomerase E

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
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
D [auth E]IPR019775WD40 repeat, conserved siteConserved Site
D [auth E]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
D [auth E]IPR001680WD40 repeatRepeat
D [auth E]IPR020472G-protein beta WD-40 repeatRepeat
D [auth E]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
F [auth J]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
F [auth J]IPR003107HAT (Half-A-TPR) repeatRepeat
F [auth J]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
G [auth L]IPR047240Pre-mRNA splicing factor component CDC5L/Cef1, second SANT/myb-like domainDomain
G [auth L]IPR017930Myb domainDomain
G [auth L]IPR009057Homeobox-like domain superfamilyHomologous Superfamily
G [auth L]IPR047242Pre-mRNA splicing factor component CDC5L/Cef1Family
G [auth L]IPR001005SANT/Myb domainDomain
G [auth L]IPR021786Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminalDomain
H [auth M]IPR013260mRNA splicing factor SYF2Family
I [auth N]IPR001748Pre-mRNA-splicing factor BUD31Family
I [auth N]IPR018230BUD31/G10-related, conserved siteConserved Site
J [auth O]IPR036855Zinc finger, CCCH-type superfamilyHomologous Superfamily
J [auth O]IPR039171Pre-mRNA-splicing factor Cwc2/Slt11Family
J [auth O]IPR000504RNA recognition motif domainDomain
J [auth O]IPR000571Zinc finger, CCCH-typeDomain
J [auth O]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
J [auth O]IPR048995STL11/RBM22-like, N-terminal domainDomain
J [auth O]IPR035979RNA-binding domain superfamilyHomologous Superfamily
K [auth P]IPR006973Pre-mRNA-splicing factor Cwf15/Cwc15Family
L [auth R]IPR017862SKI-interacting protein, SKIPFamily
L [auth R]IPR004015SKI-interacting protein SKIP, SNW domainDomain
M [auth S]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
M [auth S]IPR024936Cyclophilin-type peptidyl-prolyl cis-trans isomeraseFamily
M [auth S]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
M [auth S]IPR044666Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-likeFamily
M [auth S]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
N [auth T]IPR019775WD40 repeat, conserved siteConserved Site
N [auth T]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
N [auth T]IPR045241WD repeat Prp46/PLRG1-likeFamily
N [auth T]IPR001680WD40 repeatRepeat
N [auth T]IPR020472G-protein beta WD-40 repeatRepeat
N [auth T]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
O [auth W]IPR019775WD40 repeat, conserved siteConserved Site
O [auth W]IPR032847Pre-mRNA-processing factor 17Family
O [auth W]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
O [auth W]IPR001680WD40 repeatRepeat
O [auth W]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
R [auth U]IPR040194Cwf19-like proteinFamily
R [auth U]IPR006768Cwf19-like, C-terminal domain-1Domain
R [auth U]IPR036265HIT-like superfamilyHomologous Superfamily
R [auth U]IPR006767Cwf19-like protein, C-terminal domain-2Domain
S [auth I]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
S [auth I]IPR003107HAT (Half-A-TPR) repeatRepeat
S [auth I]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
S [auth I]IPR019734Tetratricopeptide repeatRepeat
FA [auth h],
T [auth a]		IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
FA [auth h],
T [auth a]		IPR034099Small nuclear ribonucleoprotein Sm D3Family
FA [auth h],
T [auth a]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
FA [auth h],
T [auth a]		IPR047575Sm domainDomain
FA [auth h],
T [auth a]		IPR010920LSM domain superfamilyHomologous Superfamily
GA [auth i],
U [auth b]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
GA [auth i],
U [auth b]		IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
GA [auth i],
U [auth b]		IPR047575Sm domainDomain
GA [auth i],
U [auth b]		IPR010920LSM domain superfamilyHomologous Superfamily
HA [auth j],
V [auth c]		IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
HA [auth j],
V [auth c]		IPR034102Small nuclear ribonucleoprotein D1Domain
HA [auth j],
V [auth c]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
HA [auth j],
V [auth c]		IPR047575Sm domainDomain
HA [auth j],
V [auth c]		IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth k],
W [auth d]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
IA [auth k],
W [auth d]		IPR047575Sm domainDomain
IA [auth k],
W [auth d]		IPR027248Small nuclear ribonucleoprotein Sm D2Family
IA [auth k],
W [auth d]		IPR010920LSM domain superfamilyHomologous Superfamily
JA [auth m],
X [auth f]		IPR016487Sm-like protein Lsm6/SmFFamily
JA [auth m],
X [auth f]		IPR034100Small nuclear ribonucleoprotein FFamily
JA [auth m],
X [auth f]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
JA [auth m],
X [auth f]		IPR047575Sm domainDomain
JA [auth m],
X [auth f]		IPR010920LSM domain superfamilyHomologous Superfamily
KA [auth l],
Y [auth e]		IPR027078Small nuclear ribonucleoprotein EFamily
KA [auth l],
Y [auth e]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
KA [auth l],
Y [auth e]		IPR047575Sm domainDomain
KA [auth l],
Y [auth e]		IPR010920LSM domain superfamilyHomologous Superfamily
LA [auth n],
Z [auth g]		IPR044641Sm-like protein Lsm7/SmGFamily
LA [auth n],
Z [auth g]		IPR034098Small nuclear ribonucleoprotein GFamily
LA [auth n],
Z [auth g]		IPR001163Sm domain, eukaryotic/archaea-typeDomain
LA [auth n],
Z [auth g]		IPR047575Sm domainDomain
LA [auth n],
Z [auth g]		IPR010920LSM domain superfamilyHomologous Superfamily
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR013915Pre-mRNA-splicing factor 19Domain
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR019775WD40 repeat, conserved siteConserved Site
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR038959Pre-mRNA-processing factor 19Family
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR003613U-box domainDomain
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR001680WD40 repeatRepeat
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		IPR020472G-protein beta WD-40 repeatRepeat
EA [auth K]IPR008409Pre-mRNA-splicing factor SPF27Family
MA [auth o]IPR001611Leucine-rich repeatRepeat
MA [auth o]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
MA [auth o]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
NA [auth p]IPR034562U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2Domain
NA [auth p]IPR000504RNA recognition motif domainDomain
NA [auth p]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
NA [auth p]IPR035979RNA-binding domain superfamilyHomologous Superfamily
NA [auth p]IPR034564U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1Domain
OA [auth Q]IPR048966RNA helicase aquarius, beta-barrelDomain
OA [auth Q]IPR048967RNA helicase aquarius, insertion domainDomain
OA [auth Q]IPR041677DNA2/NAM7 helicase, helicase domainDomain
OA [auth Q]IPR026300CWF11 familyFamily
OA [auth Q]IPR045055DNA2/NAM7-like helicaseFamily
OA [auth Q]IPR032174RNA helicase aquarius, N-terminal domainDomain
OA [auth Q]IPR041679DNA2/NAM7 helicase-like, C-terminalDomain
OA [auth Q]IPR047187Upf1-like, C-terminal helicase domainDomain
OA [auth Q]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
PA [auth y]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
PA [auth y]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
PA [auth y]IPR034168Peptidyl-prolyl cis-trans isomerase E, RNA recognition motifDomain
PA [auth y]IPR016304Peptidyl-prolyl cis-trans isomerase EFamily
PA [auth y]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
PA [auth y]IPR000504RNA recognition motif domainDomain
PA [auth y]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
PA [auth y]IPR035979RNA-binding domain superfamilyHomologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
Pharos:  Q6P2Q9
Pharos:  Q15029
D [auth E]Pharos:  Q96DI7
F [auth J]Pharos:  Q9BZJ0
G [auth L]Pharos:  Q99459
H [auth M]Pharos:  O95926
I [auth N]Pharos:  P41223
J [auth O]Pharos:  Q9NW64
K [auth P]Pharos:  Q9P013
L [auth R]Pharos:  Q13573
M [auth S]Pharos:  Q9Y3C6
N [auth T]Pharos:  O43660
O [auth W]Pharos:  O60508
R [auth U]Pharos:  Q2TBE0
S [auth I]Pharos:  Q9HCS7
FA [auth h],
T [auth a]		Pharos:  P62318
GA [auth i],
U [auth b]		Pharos:  P14678
HA [auth j],
V [auth c]		Pharos:  P62314
IA [auth k],
W [auth d]		Pharos:  P62316
JA [auth m],
X [auth f]		Pharos:  P62306
KA [auth l],
Y [auth e]		Pharos:  P62304
LA [auth n],
Z [auth g]		Pharos:  P62308
AA [auth q],
BA [auth r],
CA [auth s],
DA [auth t]		Pharos:  Q9UMS4
EA [auth K]Pharos:  O75934
NA [auth p]Pharos:  P08579
OA [auth Q]Pharos:  O60306
PA [auth y]Pharos:  Q9UNP9

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
L [auth R]SEP Parent Component: SER

RESID:  AA0037

PSI-MOD :  O-phospho-L-serine MOD:00046