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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
J [auth R]d3jcmr_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D3 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
Q [auth J]d3jcmj_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D3 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
K [auth S]d3jcms_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP B core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
R [auth O]d3jcmo_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP B core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
L [auth T]d3jcmt_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D1 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
S [auth P]d3jcmp_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D1 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
M [auth U]d3jcmu_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D2 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
T [auth Q]d3jcmq_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP D2 core SNRNP protein (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
N [auth V]d3jcmv_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP Small nuclear ribonucleoprotein E (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
U [auth Y]d3jcmy_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP Small nuclear ribonucleoprotein E (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
O [auth W]d3jcmw_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP Small nuclear ribonucleoprotein F, Smf (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
V [auth Z]d3jcmz_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP Small nuclear ribonucleoprotein F, Smf (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)
P [auth X]d3jcmx_ All beta proteins Sm-like fold Sm-like ribonucleoproteins Sm motif of small nuclear ribonucleoproteins, SNRNP Small nuclear ribonucleoprotein G (Saccharomyces cerevisiae S288C ) [TaxId: 559292 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyJAB1/MPN domain-like8053281 3001105 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyRibonuclease H-like8040983 3000143 SCOP2B (2022-06-29)
F [auth L]SCOP2B SuperfamilyThioredoxin-like8083616 3000031 SCOP2B (2022-06-29)
G [auth M]SCOP2B SuperfamilyL30e-like8033484 3001739 SCOP2B (2022-06-29)
J [auth R]SCOP2B SuperfamilySm-like ribonucleoproteins8098694 3000419 SCOP2B (2022-06-29)
Q [auth J]SCOP2B SuperfamilySm-like ribonucleoproteins8098694 3000419 SCOP2B (2022-06-29)
S [auth P]SCOP2 FamilySm motif of small nuclear ribonucleoproteins SNRNP8082630 4001809 SCOP2 (2022-06-29)
S [auth P]SCOP2 SuperfamilySm-like ribonucleoproteins8082631 3000419 SCOP2 (2022-06-29)
M [auth U]SCOP2B SuperfamilySm-like ribonucleoproteins8063490 3000419 SCOP2B (2022-06-29)
T [auth Q]SCOP2B SuperfamilySm-like ribonucleoproteins8063490 3000419 SCOP2B (2022-06-29)
O [auth W]SCOP2B SuperfamilySm-like ribonucleoproteins8043703 3000419 SCOP2B (2022-06-29)
V [auth Z]SCOP2B SuperfamilySm-like ribonucleoproteins8043703 3000419 SCOP2B (2022-06-29)
P [auth X]SCOP2B SuperfamilySm-like ribonucleoproteins8098668 3000419 SCOP2B (2022-06-29)
W [auth a]SCOP2B SuperfamilySm-like ribonucleoproteins8098668 3000419 SCOP2B (2022-06-29)
Z [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8063446 3000419 SCOP2B (2022-06-29)
AA [auth e]SCOP2B SuperfamilySm-like ribonucleoproteins8099110 3000419 SCOP2B (2022-06-29)
BA [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8063464 3000419 SCOP2B (2022-06-29)
CA [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8063498 3000419 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF10596,PF10597e3jcmA3 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,PF08083e3jcmA1 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)
APF10598e3jcmA2 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)
APF08084e3jcmA5 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF08084ECOD (1.6)
APF10596e3jcmA6 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
APF12134e3jcmA4 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
BPF00400e3jcmB3 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
C [auth I]PF01798e3jcmI1 A: alpha arraysX: HhH/H2THH: SAM/DNA-glycosylaseT: Nop C-terminal domainF: PF01798ECOD (1.6)
C [auth I]PF01798e3jcmI3 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)
C [auth I]PF09785e3jcmI2 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)
D [auth G]F_UNCLASSIFIEDe3jcmG1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
E [auth K]PF06544e3jcmK1 A: a+b two layersX: Alpha-beta plaitsH: Acylphosphatase-like (From Topology)T: Acylphosphatase-likeF: PF06544ECOD (1.6)
E [auth K]PF08572e3jcmK2 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)
F [auth L]PF02966e3jcmL1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PF02966ECOD (1.6)
G [auth M]PF01248e3jcmM1 A: a+b three layersX: Bacillus chorismate mutase-likeH: L30e-like (From Topology)T: L30e-likeF: PF01248ECOD (1.6)
HF_UNCLASSIFIEDe3jcmH2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: F_UNCLASSIFIEDECOD (1.6)
HPF03764e3jcmH5 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)
HF_UNCLASSIFIEDe3jcmH4 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: F_UNCLASSIFIEDECOD (1.6)
HPF00679e3jcmH3 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)
HPF00009e3jcmH1 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 N]PF02889e3jcmN7 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: PF02889ECOD (1.6)
I [auth N]F_UNCLASSIFIEDe3jcmN5 A: alpha arraysX: HTHH: HTHT: wingedF: F_UNCLASSIFIEDECOD (1.6)
I [auth N]F_UNCLASSIFIEDe3jcmN3 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)
I [auth N]PF02889e3jcmN6 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)
I [auth N]F_UNCLASSIFIEDe3jcmN1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: F_UNCLASSIFIEDECOD (1.6)
I [auth N]PF00270e3jcmN8 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00270ECOD (1.6)
I [auth N]PF00271e3jcmN10 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00271ECOD (1.6)
J [auth R]PF01423e3jcmR1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Q [auth J]PF01423e3jcmJ1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
K [auth S]PF01423e3jcmS1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
R [auth O]PF01423e3jcmO1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
L [auth T]PF01423e3jcmT1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
S [auth P]PF01423e3jcmP1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
M [auth U]PF01423e3jcmU1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
T [auth Q]PF01423e3jcmQ1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
N [auth V]PF01423e3jcmV1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
U [auth Y]PF01423e3jcmY1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
O [auth W]PF01423e3jcmW1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
V [auth Z]PF01423e3jcmZ1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
P [auth X]PF01423e3jcmX1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
W [auth a]PF01423e3jcma1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
X [auth b]PF01423e3jcmb1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Y [auth c]PF01423e3jcmc1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Z [auth d]PF01423e3jcmd1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
AA [auth e]PF01423e3jcme1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BA [auth f]PF01423e3jcmf1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
CA [auth g]PF01423e3jcmg1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
DA [auth h]PF01423e3jcmh1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
F [auth L]3.40.30.10 Alpha Beta 3-Layer(aba) Sandwich Glutaredoxin GlutaredoxinCATH (4.3.0)
G [auth M]3.30.1330.30 Alpha Beta 2-Layer Sandwich 60s Ribosomal Protein L30 Chain: ACATH (4.3.0)
H3.30.70.870 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits Elongation Factor G (Translational Gtpase), domain 3CATH (4.3.0)
I [auth N]3.40.50.300 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold P-loop containing nucleotide triphosphate hydrolasesCATH (4.3.0)
I [auth N]1.10.10.10 Mainly Alpha Orthogonal Bundle Arc Repressor Mutant, subunit A Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domainCATH (4.3.0)
I [auth N]1.10.3380.10 Mainly Alpha Orthogonal Bundle Sec63 N-terminal domain-like fold Sec63 N-terminal domain-like domainCATH (4.3.0)
I [auth N]1.10.150.20 Mainly Alpha Orthogonal Bundle DNA polymerase domain 1CATH (4.3.0)
I [auth N]2.60.40.150 Mainly Beta Sandwich Immunoglobulin-like C2 domainCATH (4.3.0)
J [auth R]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Q [auth J]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
L [auth T]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
S [auth P]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
M [auth U]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
T [auth Q]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
N [auth V]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
U [auth Y]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
O [auth W]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
V [auth Z]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
P [auth X]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
W [auth a]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
X [auth b]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Y [auth c]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Z [auth d]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
AA [auth e]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
BA [auth f]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
CA [auth g]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
DA [auth h]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (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
PF08084PROCT (NUC072) domain (PROCT)PROCT (NUC072) domainThe PROCT domain is the C-terminal domain in pre-mRNA splicing factors of PRO8 family [1].Domain
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
C [auth I]PF09785Prp31 C terminal domain (Prp31_C)Prp31 C terminal domain- Family
C [auth I]PF01798snoRNA binding domain, fibrillarin (Nop)snoRNA binding domain, fibrillarin- Family
D [auth G]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
E [auth K]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
E [auth K]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
F [auth L]PF02966Mitosis protein DIM1 (DIM1)Mitosis protein DIM1- Domain
G [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
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
PF16004116 kDa U5 small nuclear ribonucleoprotein component N-terminus (EFTUD2)116 kDa U5 small nuclear ribonucleoprotein component N-terminus- Family
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
I [auth N]PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
I [auth N]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
I [auth N]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
J [auth R],
Q [auth J]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
K [auth S],
R [auth O]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
L [auth T],
S [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
M [auth U],
T [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
N [auth V],
U [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
O [auth W],
V [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
P [auth X],
W [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
X [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
Y [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
Z [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
AA [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
BA [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
CA [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
DA [auth h]PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Pre-mRNA-splicing factor 8
U4/U6 small nuclear ribonucleoprotein PRP4
C [auth I]Pre-mRNA-processing factor 31
D [auth G]Pre-mRNA-splicing factor 6-
E [auth K]U4/U6 small nuclear ribonucleoprotein PRP3-
F [auth L]Spliceosomal protein DIB1-
G [auth M]13 kDa ribonucleoprotein-associated protein
Pre-mRNA-splicing factor SNU114
I [auth N]Pre-mRNA-splicing helicase BRR2
J [auth R],
Q [auth J]
Small nuclear ribonucleoprotein Sm D3
K [auth S],
R [auth O]
Small nuclear ribonucleoprotein-associated protein B
L [auth T],
S [auth P]
Small nuclear ribonucleoprotein Sm D1
M [auth U],
T [auth Q]
Small nuclear ribonucleoprotein Sm D2
N [auth V],
U [auth Y]
Small nuclear ribonucleoprotein E
O [auth W],
V [auth Z]
Small nuclear ribonucleoprotein F
P [auth X],
W [auth a]
Small nuclear ribonucleoprotein G
X [auth b]U6 snRNA-associated Sm-like protein LSm8
Y [auth c]U6 snRNA-associated Sm-like protein LSm2
Z [auth d]U6 snRNA-associated Sm-like protein LSm3
AA [auth e]U6 snRNA-associated Sm-like protein LSm6
BA [auth f]U6 snRNA-associated Sm-like protein LSm5
CA [auth g]U6 snRNA-associated Sm-like protein LSm7
DA [auth h]U6 snRNA-associated Sm-like protein LSm4
EA [auth C]pre-mRNA---
FA [auth D]SNR6 snRNA---
GA [auth E]SNR14 snRNA---
HA [auth F]SNR7-L snRNA---

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
IPR019775WD40 repeat, conserved siteConserved Site
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
IPR014906Pre-mRNA processing factor 4 (PRP4)-likeDomain
IPR001680WD40 repeatRepeat
IPR020472G-protein beta WD-40 repeatRepeat
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
C [auth I]IPR042239Nop, C-terminal domainHomologous Superfamily
C [auth I]IPR019175Prp31 C-terminalDomain
C [auth I]IPR002687Nop domainDomain
C [auth I]IPR012976NOSICDomain
C [auth I]IPR027105U4/U6 small nuclear ribonucleoprotein Prp31Family
C [auth I]IPR036070Nop domain superfamilyHomologous Superfamily
D [auth G]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
D [auth G]IPR010491PRP1 splicing factor, N-terminalDomain
D [auth G]IPR003107HAT (Half-A-TPR) repeatRepeat
D [auth G]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
D [auth G]IPR019734Tetratricopeptide repeatRepeat
E [auth K]IPR013881Pre-mRNA-splicing factor 3 domainDomain
E [auth K]IPR027104U4/U6 small nuclear ribonucleoprotein Prp3Family
E [auth K]IPR010541Small nuclear ribonucleoprotein Prp3, C-terminal domainDomain
F [auth L]IPR004123Dim1 familyFamily
F [auth L]IPR036249Thioredoxin-like superfamilyHomologous Superfamily
G [auth M]IPR002415H/ACA ribonucleoprotein complex, subunit Nhp2-likeFamily
G [auth M]IPR029064Ribosomal protein eL30-like superfamilyHomologous Superfamily
G [auth M]IPR018492Ribosomal protein eL8/Nhp2 familyFamily
G [auth M]IPR004038Ribosomal protein eL8/eL30/eS12/Gadd45Domain
G [auth M]IPR004037Large ribosomal subunit protein eL8-like, conserved siteConserved Site
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
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
I [auth N]IPR001650Helicase, C-terminal domain-likeDomain
I [auth N]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
I [auth N]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
I [auth N]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
I [auth N]IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
I [auth N]IPR041094Brr2, N-terminal helicase PWI domainDomain
I [auth N]IPR004179Sec63 domainDomain
I [auth N]IPR035892C2 domain superfamilyHomologous Superfamily
I [auth N]IPR014756Immunoglobulin E-setHomologous Superfamily
I [auth N]IPR011545DEAD/DEAH box helicase domainDomain
I [auth N]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
J [auth R],
Q [auth J]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
J [auth R],
Q [auth J]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
J [auth R],
Q [auth J]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
J [auth R],
Q [auth J]
IPR047575Sm domainDomain
J [auth R],
Q [auth J]
IPR010920LSM domain superfamilyHomologous Superfamily
K [auth S],
R [auth O]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
K [auth S],
R [auth O]
IPR047575Sm domainDomain
K [auth S],
R [auth O]
IPR010920LSM domain superfamilyHomologous Superfamily
L [auth T],
S [auth P]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
L [auth T],
S [auth P]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
L [auth T],
S [auth P]
IPR047575Sm domainDomain
L [auth T],
S [auth P]
IPR010920LSM domain superfamilyHomologous Superfamily
M [auth U],
T [auth Q]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
M [auth U],
T [auth Q]
IPR047575Sm domainDomain
M [auth U],
T [auth Q]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
M [auth U],
T [auth Q]
IPR010920LSM domain superfamilyHomologous Superfamily
N [auth V],
U [auth Y]
IPR027078Small nuclear ribonucleoprotein EFamily
N [auth V],
U [auth Y]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
N [auth V],
U [auth Y]
IPR047575Sm domainDomain
N [auth V],
U [auth Y]
IPR010920LSM domain superfamilyHomologous Superfamily
O [auth W],
V [auth Z]
IPR016487Sm-like protein Lsm6/SmFFamily
O [auth W],
V [auth Z]
IPR034100Small nuclear ribonucleoprotein FFamily
O [auth W],
V [auth Z]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
O [auth W],
V [auth Z]
IPR047575Sm domainDomain
O [auth W],
V [auth Z]
IPR010920LSM domain superfamilyHomologous Superfamily
P [auth X],
W [auth a]
IPR044641Sm-like protein Lsm7/SmGFamily
P [auth X],
W [auth a]
IPR034098Small nuclear ribonucleoprotein GFamily
P [auth X],
W [auth a]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
P [auth X],
W [auth a]
IPR047575Sm domainDomain
P [auth X],
W [auth a]
IPR010920LSM domain superfamilyHomologous Superfamily
X [auth b]IPR001163Sm domain, eukaryotic/archaea-typeDomain
X [auth b]IPR047575Sm domainDomain
X [auth b]IPR034103Sm-like protein Lsm8Domain
X [auth b]IPR010920LSM domain superfamilyHomologous Superfamily
X [auth b]IPR044642U6 snRNA-associated Sm-like protein Lsm1/8Family
Y [auth c]IPR001163Sm domain, eukaryotic/archaea-typeDomain
Y [auth c]IPR047575Sm domainDomain
Y [auth c]IPR010920LSM domain superfamilyHomologous Superfamily
Y [auth c]IPR016654U6 snRNA-associated Sm-like protein LSm2Family
Z [auth d]IPR040002U6 snRNA-associated Sm-like protein Lsm3Family
Z [auth d]IPR001163Sm domain, eukaryotic/archaea-typeDomain
Z [auth d]IPR047575Sm domainDomain
Z [auth d]IPR010920LSM domain superfamilyHomologous Superfamily
Z [auth d]IPR034105Sm-like protein Lsm3Domain
AA [auth e]IPR001163Sm domain, eukaryotic/archaea-typeDomain
AA [auth e]IPR047575Sm domainDomain
AA [auth e]IPR016487Sm-like protein Lsm6/SmFFamily
AA [auth e]IPR010920LSM domain superfamilyHomologous Superfamily
BA [auth f]IPR001163Sm domain, eukaryotic/archaea-typeDomain
BA [auth f]IPR047575Sm domainDomain
BA [auth f]IPR033871Sm-like protein LSm5Domain
BA [auth f]IPR010920LSM domain superfamilyHomologous Superfamily
CA [auth g]IPR044641Sm-like protein Lsm7/SmGFamily
CA [auth g]IPR017132Sm-like protein Lsm7Family
CA [auth g]IPR001163Sm domain, eukaryotic/archaea-typeDomain
CA [auth g]IPR047575Sm domainDomain
CA [auth g]IPR010920LSM domain superfamilyHomologous Superfamily
DA [auth h]IPR001163Sm domain, eukaryotic/archaea-typeDomain
DA [auth h]IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
DA [auth h]IPR047575Sm domainDomain
DA [auth h]IPR034101Sm-like protein Lsm4Domain
DA [auth h]IPR010920LSM domain superfamilyHomologous Superfamily