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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Gd5o9zg_ All alpha proteins alpha-alpha superhelix TPR-like Tetratricopeptide repeat (TPR) Pre-mRNA splicing factor 6 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Kd5o9zk_ Peptides Microfibrillar-associated protein 1 fragment Microfibrillar-associated protein 1 fragment Microfibrillar-associated protein 1 fragment Microfibrillar-associated protein 1 fragment (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Pd5o9zp_ Peptides Pre-mRNA splicing factor Snu66-like Pre-mRNA splicing factor Snu66-like Pre-mRNA splicing factor Sart1 / Snu66-like Pre-mRNA splicing factor Sart1 / Snu66 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
NA [auth v]d5o9zv_ All alpha proteins alpha-alpha superhelix ARM repeat HEAT repeat Splicing factor 3B subunit 1, HEAT repeats (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
PA [auth x]d5o9zx_ Peptides Splicing factor 3B subunit 5 fragment Splicing factor 3B subunit 5 fragment Splicing factor 3B subunit 5 fragment Splicing factor 3B subunit 5 fragment (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
QA [auth y]d5o9zy_ Small proteins Triquetra knot Pre-mRNA splicing factor Phf5-like Pre-mRNA splicing factor Phf5-like Pre-mRNA splicing factor Phf5 / Rds3 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed5o9ze2 Alpha and beta proteins (a+b) Ferredoxin-like Acylphosphatase/BLUF domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 C-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed5o9ze1 Peptides Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 N-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 N-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 N-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp3 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Hd5o9zh2 All alpha proteins Nop domain Nop domain Nop domain U4/U6 small nuclear ribonucleoprotein Prp31 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Hd5o9zh1 Peptides Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp31 C-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp31 C-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp31 C-terminal domain-like Spliceosomal U4/U6 small nuclear ribonucleoprotein Prp31 (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Id5o9zi_ All alpha proteins alpha-alpha superhelix Pre-mRNA splicing factor Prp38 N-terminal-like Pre-mRNA splicing factor Prp38-like Pre-mRNA splicing factor Prp38A (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)
ASCOP2B SuperfamilyJAB1/MPN domain-like8053277 3001105 SCOP2B (2022-06-29)
JSCOP2B SuperfamilyThioredoxin-like8044390 3000031 SCOP2B (2022-06-29)
OSCOP2B SuperfamilyL30e-like8043738 3001739 SCOP2B (2022-06-29)
AA [auth i]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
T [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
UA [auth T]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
CA [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
V [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
WA [auth V]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
DA [auth l]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
W [auth e]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
XA [auth W]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
EA [auth m]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
YA [auth X]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
X [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
FA [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
Y [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
ZA [auth Z]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
IA [auth q]SCOP2B SuperfamilySm-like ribonucleoproteins8063488 3000419 SCOP2B (2022-06-29)
JA [auth r]SCOP2B SuperfamilySm-like ribonucleoproteins8063472 3000419 SCOP2B (2022-06-29)
KA [auth s]SCOP2B SuperfamilySm-like ribonucleoproteins8063442 3000419 SCOP2B (2022-06-29)
LA [auth t]SCOP2B SuperfamilySm-like ribonucleoproteins8063466 3000419 SCOP2B (2022-06-29)
OA [auth w]SCOP2B SuperfamilyWD40 repeat-like8052535 3001694 SCOP2B (2022-06-29)
OA [auth w]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
OA [auth w]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
OA [auth w]SCOP2B SuperfamilyWD40 repeat-like8051197 3001694 SCOP2B (2022-06-29)
QA [auth y]SCOP2B SuperfamilyTriquetra zinc finger motif8051848 3002040 SCOP2B (2022-06-29)
RA [auth z]SCOP2B SuperfamilyL domain-like8043993 3001010 SCOP2B (2022-06-29)
SA [auth 1]SCOP2B SuperfamilyRNA-binding domain RBD8035327 3000110 SCOP2B (2022-06-29)
MSCOP2B SuperfamilyCyclophilin-like8042789 3000168 SCOP2B (2022-06-29)
S [auth a]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
TA [auth S]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
Z [auth h]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
U [auth c]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
VA [auth U]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
BA [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
HA [auth p]SCOP2B SuperfamilySm-like ribonucleoproteins8063456 3000419 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyBrl domain-like8036193 3000115 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyE set domains8055093 3000070 SCOP2B (2022-06-29)
MA [auth u]SCOP2B SuperfamilySm-like ribonucleoproteins8063492 3000419 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyNop domain8033305 3001551 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyPRP38-like8055808 3002318 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF10596,PF10597e5o9zA3 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,PF08083e5o9zA6 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)
APF10598e5o9zA1 A: a+b two layersX: Alpha-beta plaitsH: Adenylyl and guanylyl cyclase catalytic domain-likeT: Adenylyl and guanylyl cyclase catalytic domain-likeF: PF10598ECOD (1.6)
APF01398,PF08084e5o9zA4 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398,PF08084ECOD (1.6)
APF10596e5o9zA2 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
APF12134e5o9zA5 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
JPF02966e5o9zJ1 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: PF02966ECOD (1.6)
NPF12171e5o9zN1 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF12171ECOD (1.6)
OPF01248e5o9zO1 A: a+b three layersX: Bacillus chorismate mutase-likeH: L30e-like (From Topology)T: L30e-likeF: PF01248ECOD (1.6)
QPF06220e5o9zQ1 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF06220ECOD (1.6)
AA [auth i]PF01423e5o9zi1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
T [auth b]PF01423e5o9zb1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
CA [auth k]PF01423e5o9zk1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
V [auth d]PF01423e5o9zd1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
DA [auth l]PF01423e5o9zl1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
W [auth e]PF01423e5o9ze1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
EA [auth m]PF01423e5o9zm1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
X [auth f]PF01423e5o9zf1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
FA [auth n]PF01423e5o9zn1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Y [auth g]PF01423e5o9zg1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
OA [auth w]PF03178,PF10433e5o9zw1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF03178,PF10433ECOD (1.6)
OA [auth w]PF10433e5o9zw4 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF10433ECOD (1.6)
OA [auth w]PF03178e5o9zw3 A: alpha arraysX: HTHH: HTHT: tri-helicalF: PF03178ECOD (1.6)
MPF00160e5o9zM1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: PF00160ECOD (1.6)
S [auth a]PF01423e5o9za1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
Z [auth h]PF01423e5o9zh1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BPF03144e5o9zB5 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF03144ECOD (1.6)
BPF03764e5o9zB4 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)
BPF00679e5o9zB2 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)
BPF14492e5o9zB1 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)
BPF00009e5o9zB3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00009ECOD (1.6)
U [auth c]PF01423e5o9zc1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BA [auth j]PF01423e5o9zj1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
CPF02889e5o9zC8 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: PF02889ECOD (1.6)
CF_UNCLASSIFIEDe5o9zC4 A: alpha arraysX: HTHH: HTHT: wingedF: F_UNCLASSIFIEDECOD (1.6)
CF_UNCLASSIFIEDe5o9zC6 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)
CPF02889e5o9zC11 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)
CPF00270e5o9zC1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00270ECOD (1.6)
CPF00271e5o9zC10 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00271ECOD (1.6)
IPF03371e5o9zI1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Pre-mRNA-splicing factor 38A (From Topology)T: Pre-mRNA-splicing factor 38AF: PF03371ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF10597U5-snRNA binding site 2 of PrP8 (U5_2-snRNA_bdg)U5-snRNA binding site 2 of PrP8The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis [1]. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that ...The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis [1]. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that Prp8 could directly affect the function of the catalytic core, perhaps acting as a splicing cofactor [2].
Domain
PF10598RNA recognition motif of the spliceosomal PrP8 (RRM_4)RNA recognition motif of the spliceosomal PrP8The large RNA-protein complex of the spliceosome catalyses pre-mRNA splicing. One of the most conserved core proteins is PrP8 which occupies a central position in the catalytic core of the spliceosome, and has been implicated in several crucial molec ...The large RNA-protein complex of the spliceosome catalyses pre-mRNA splicing. One of the most conserved core proteins is PrP8 which occupies a central position in the catalytic core of the spliceosome, and has been implicated in several crucial molecular rearrangements that occur there, and has recently come under the spotlight for its role in the inherited human disease, Retinitis Pigmentosa [1]. The RNA-recognition motif of PrP8 is highly conserved and provides a possible RNA binding centre for the 5-prime SS, BP, or 3-prime SS of pre-mRNA which are known to contact with Prp8. The most conserved regions of an RRM are defined as the RNP1 and RNP2 sequences. Recognition of RNA targets can also be modulated by a number of other factors, most notably the two loops beta1-alpha1, beta2-beta3 and the amino acid residues C-terminal to the RNP2 domain [2].
Domain
PF10596U6-snRNA interacting domain of PrP8 (U6-snRNA_bdg)U6-snRNA interacting domain of PrP8This domain incorporates the interacting site for the U6-snRNA as part of the U4/U6.U5 tri-snRNPs complex of the spliceosome, and is the prime candidate for the role of cofactor for the spliceosome's RNA core. The essential spliceosomal protein Prp8 ...This domain incorporates the interacting site for the U6-snRNA as part of the U4/U6.U5 tri-snRNPs complex of the spliceosome, and is the prime candidate for the role of cofactor for the spliceosome's RNA core. The essential spliceosomal protein Prp8 interacts with U5 and U6 snRNAs and with specific pre-mRNA sequences that participate in catalysis. This close association with crucial RNA sequences, together with extensive genetic evidence, suggests that Prp8 could directly affect the function of the catalytic core, perhaps acting as a splicing cofactor [1].
Domain
PF12134PRP8 domain IV core (PRP8_domainIV)PRP8 domain IV coreThis domain is found in eukaryotes, and is about 20 amino acids in length. It is found associated with Pfam:PF10597, Pfam:PF10596, Pfam:PF10598, Pfam:PF08083, Pfam:PF08082, Pfam:PF01398, Pfam:PF08084. There is a conserved LILR sequence motif. The dom ...This domain is found in eukaryotes, and is about 20 amino acids in length. It is found associated with Pfam:PF10597, Pfam:PF10596, Pfam:PF10598, Pfam:PF08083, Pfam:PF08082, Pfam:PF01398, Pfam:PF08084. There is a conserved LILR sequence motif. The domain is a selenomethionine domain in a subunit of the spliceosome. The function of PRP8 domain IV is believed to be interaction with the splicosomal core.
Domain
PF08082PRO8NT (NUC069), PrP8 N-terminal domain (PRO8NT)PRO8NT (NUC069), PrP8 N-terminal domainThe PRO8NT domain is found at the N-terminus of pre-mRNA splicing factors of PRO8 family [1]. The NLS or nuclear localisation signal for these spliceosome proteins begins at the start and runs for 60 residues. N-terminal to this domain is a highly va ...The PRO8NT domain is found at the N-terminus of pre-mRNA splicing factors of PRO8 family [1]. The NLS or nuclear localisation signal for these spliceosome proteins begins at the start and runs for 60 residues. N-terminal to this domain is a highly variable proline-rich region [4].
Domain
PF08083PROCN (NUC071) domain (PROCN)PROCN (NUC071) domainThe PROCN domain is the central domain in pre-mRNA splicing factors of PRO8 family [1].Domain
PF08084PROCT (NUC072) domain (PROCT)PROCT (NUC072) domainThe PROCT domain is the C-terminal domain in pre-mRNA splicing factors of PRO8 family [1].Domain
PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
PF08799pre-mRNA processing factor 4 (PRP4) like (PRP4)pre-mRNA processing factor 4 (PRP4) likeThis small domain is found on PRP4 ribonuleoproteins. PRP4 is a U4/U6 small nuclear ribonucleoprotein that is involved in pre-mRNA processing.Domain
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
PF14559Tetratricopeptide repeat (TPR_19)Tetratricopeptide repeat- Repeat
PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
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
PF02966Mitosis protein DIM1 (DIM1)Mitosis protein DIM1- Domain
PF06991Microfibril-associated/Pre-mRNA processing (MFAP1)Microfibril-associated/Pre-mRNA processing- Family
PF17814LisH-like dimerisation domain (LisH_TPL)LisH-like dimerisation domainTOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif [1].Domain
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
PF12171Zinc-finger double-stranded RNA-binding (zf-C2H2_jaz)Zinc-finger double-stranded RNA-binding- Family
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
PF03343SART-1 family (SART-1)SART-1 family- Family
PF06220U1 zinc finger (zf-U1)U1 zinc fingerThis family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class o ...This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class of weak 5' ss is promoted by binding of the protein TIA-1 to uridine-rich sequences immediately downstream from the 5' ss. Binding of TIA-1 in the vicinity of a 5' ss helps to stabilise U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator [1]. This domain is probably a zinc-binding. It is found in multiple copies in some members of the family.
Domain
PF07808RED-like protein N-terminal region (RED_N)RED-like protein N-terminal region- Family
AA [auth i],
T [auth b],
UA [auth T]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
CA [auth k],
V [auth d],
WA [auth V]
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 l],
W [auth e],
XA [auth W]
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
EA [auth m],
X [auth f],
YA [auth X]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
FA [auth n],
Y [auth g],
ZA [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
IA [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
JA [auth r]PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
KA [auth s]PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
LA [auth t]PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
OA [auth w]PF10433Mono-functional DNA-alkylating methyl methanesulfonate N-term (MMS1_N)Mono-functional DNA-alkylating methyl methanesulfonate N-term- Repeat
OA [auth w]PF03178CPSF A subunit region (CPSF_A)CPSF A subunit region- Repeat
PA [auth x]PF07189Splicing factor 3B subunit 10 (SF3b10) (SF3b10)Splicing factor 3B subunit 10 (SF3b10)- Family
QA [auth y]PF03660PHF5-like protein (PHF5)PHF5-like protein- Family
RA [auth z]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
SA [auth 1]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
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
S [auth a],
TA [auth S],
Z [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
PF00679Elongation factor G C-terminus (EFG_C)Elongation factor G C-terminusThis domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.Domain
PF00009Elongation factor Tu GTP binding domain (GTP_EFTU)Elongation factor Tu GTP binding domainThis domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.Domain
PF14492Elongation Factor G, domain III (EFG_III)Elongation Factor G, domain IIIThis domain is found in Elongation Factor G. It shares a similar structure with domain V (Pfam:PF00679). Structural studies in drosophila indicate this is domain 3 [1].Domain
PF03144Elongation factor Tu domain 2 (GTP_EFTU_D2)Elongation factor Tu domain 2Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.
Domain
PF03764Elongation factor G, domain IV (EFG_IV)Elongation factor G, domain IVThis domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.Domain
BA [auth j],
U [auth c],
VA [auth U]
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 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
HA [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
PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
PF00270DEAD/DEAH box helicase (DEAD)DEAD/DEAH box helicaseMembers of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome ...Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Domain
PF00271Helicase conserved C-terminal domain (Helicase_C)Helicase conserved C-terminal domainThe Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.Domain
MA [auth u]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
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
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
PF09785Prp31 C terminal domain (Prp31_C)Prp31 C terminal domain- Family
PF01798snoRNA binding domain, fibrillarin (Nop)snoRNA binding domain, fibrillarin- Family
PF03371PRP38 family (PRP38)PRP38 family- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Pre-mRNA-processing-splicing factor 8
U5 small nuclear ribonucleoprotein 40 kDa protein
U4/U6 small nuclear ribonucleoprotein Prp4
Pre-mRNA-processing factor 6
Thioredoxin-like protein 4A-
Microfibrillar-associated protein 1
WD40 repeat-containing protein SMU1-
Zinc finger matrin-type protein 2
NHP2-like protein 1
U4/U6.U5 tri-snRNP-associated protein 1
WW domain-binding protein 4
Protein Red
AA [auth i],
T [auth b],
UA [auth T]
Small nuclear ribonucleoprotein F
CA [auth k],
V [auth d],
WA [auth V]
Small nuclear ribonucleoprotein G
DA [auth l],
W [auth e],
XA [auth W]
Small nuclear ribonucleoprotein Sm D3
EA [auth m],
X [auth f],
YA [auth X]
Small nuclear ribonucleoprotein-associated proteins B and B'
FA [auth n],
Y [auth g],
ZA [auth Z]
Small nuclear ribonucleoprotein Sm D1
IA [auth q]U6 snRNA-associated Sm-like protein LSm4
JA [auth r]U6 snRNA-associated Sm-like protein LSm5
KA [auth s]U6 snRNA-associated Sm-like protein LSm6
LA [auth t]U6 snRNA-associated Sm-like protein LSm7
NA [auth v]Splicing factor 3B subunit 1
OA [auth w]Splicing factor 3B subunit 3 (SF3B3)
PA [auth x]Splicing factor 3B subunit 5
QA [auth y]PHD finger-like domain-containing protein 5A
RA [auth z]U2 small nuclear ribonucleoprotein A'
SA [auth 1]U2 small nuclear ribonucleoprotein B''
BB [auth 2]Human gene for small nuclear RNA U2 (snRNA U2)---
CB [auth 4]Homo sapiens U4A snRNA---
DB [auth 5]Homo sapiens U5 A small nuclear RNA---
Peptidyl-prolyl cis-trans isomerase H
S [auth a],
TA [auth S],
Z [auth h]
Small nuclear ribonucleoprotein Sm D2
116 kDa U5 small nuclear ribonucleoprotein component
BA [auth j],
U [auth c],
VA [auth U]
Small nuclear ribonucleoprotein E
GA [auth o]U6 snRNA-associated Sm-like protein LSm2
HA [auth p]U6 snRNA-associated Sm-like protein LSm3
U5 small nuclear ribonucleoprotein 200 kDa helicase
MA [auth u]U6 snRNA-associated Sm-like protein LSm8
AB [auth Y]MINX pre-mRNA---
EB [auth 6]Homo sapiens RNA, U6 small nuclear 1 (RNU6-1), small nuclear RNA---
U4/U6 small nuclear ribonucleoprotein Prp3
U4/U6 small nuclear ribonucleoprotein Prp31
Pre-mRNA-splicing factor 38A

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
IPR001680WD40 repeatRepeat
IPR020472G-protein beta WD-40 repeatRepeat
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
IPR019775WD40 repeat, conserved siteConserved Site
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
IPR036285PRP4-like 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
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
IPR010491PRP1 splicing factor, N-terminalDomain
IPR003107HAT (Half-A-TPR) repeatRepeat
IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
IPR019734Tetratricopeptide repeatRepeat
IPR004123Dim1 familyFamily
IPR036249Thioredoxin-like superfamilyHomologous Superfamily
IPR033194Microfibrillar-associated protein 1Family
IPR009730Micro-fibrillar-associated protein 1, C-terminalDomain
IPR019775WD40 repeat, conserved siteConserved Site
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
IPR006595CTLH, C-terminal LisH motifDomain
IPR045184WD40 repeat-containing protein SMU1Family
IPR001680WD40 repeatRepeat
IPR020472G-protein beta WD-40 repeatRepeat
IPR006594LIS1 homology motifConserved Site
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
IPR040107U4/U6.U5 small nuclear ribonucleoprotein component Snu23Family
IPR022755Zinc finger, double-stranded RNA bindingDomain
IPR002415H/ACA ribonucleoprotein complex, subunit Nhp2-likeFamily
IPR029064Ribosomal protein eL30-like superfamilyHomologous Superfamily
IPR018492Ribosomal protein eL8/Nhp2 familyFamily
IPR004038Ribosomal protein eL8/eL30/eS12/Gadd45Domain
IPR004037Large ribosomal subunit protein eL8-like, conserved siteConserved Site
IPR045347HIND motifConserved Site
IPR005011SNU66/SART1 familyFamily
IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
IPR040023WW domain-binding protein 4Family
IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
IPR036020WW domain superfamilyHomologous Superfamily
IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
IPR001202WW domainDomain
IPR013085U1-C, C2H2-type zinc fingerDomain
IPR039896Protein Red-likeFamily
IPR012916RED-like, N-terminalDomain
IPR012492Protein RED, C-terminalDomain
AA [auth i],
T [auth b],
UA [auth T]
IPR016487Sm-like protein Lsm6/SmFFamily
AA [auth i],
T [auth b],
UA [auth T]
IPR034100Small nuclear ribonucleoprotein FFamily
AA [auth i],
T [auth b],
UA [auth T]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
AA [auth i],
T [auth b],
UA [auth T]
IPR047575Sm domainDomain
AA [auth i],
T [auth b],
UA [auth T]
IPR010920LSM domain superfamilyHomologous Superfamily
CA [auth k],
V [auth d],
WA [auth V]
IPR044641Sm-like protein Lsm7/SmGFamily
CA [auth k],
V [auth d],
WA [auth V]
IPR034098Small nuclear ribonucleoprotein GFamily
CA [auth k],
V [auth d],
WA [auth V]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
CA [auth k],
V [auth d],
WA [auth V]
IPR047575Sm domainDomain
CA [auth k],
V [auth d],
WA [auth V]
IPR010920LSM domain superfamilyHomologous Superfamily
DA [auth l],
W [auth e],
XA [auth W]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
DA [auth l],
W [auth e],
XA [auth W]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
DA [auth l],
W [auth e],
XA [auth W]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
DA [auth l],
W [auth e],
XA [auth W]
IPR047575Sm domainDomain
DA [auth l],
W [auth e],
XA [auth W]
IPR010920LSM domain superfamilyHomologous Superfamily
EA [auth m],
X [auth f],
YA [auth X]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
EA [auth m],
X [auth f],
YA [auth X]
IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
EA [auth m],
X [auth f],
YA [auth X]
IPR047575Sm domainDomain
EA [auth m],
X [auth f],
YA [auth X]
IPR010920LSM domain superfamilyHomologous Superfamily
FA [auth n],
Y [auth g],
ZA [auth Z]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
FA [auth n],
Y [auth g],
ZA [auth Z]
IPR034102Small nuclear ribonucleoprotein D1Domain
FA [auth n],
Y [auth g],
ZA [auth Z]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
FA [auth n],
Y [auth g],
ZA [auth Z]
IPR047575Sm domainDomain
FA [auth n],
Y [auth g],
ZA [auth Z]
IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth q]IPR001163Sm domain, eukaryotic/archaea-typeDomain
IA [auth q]IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
IA [auth q]IPR047575Sm domainDomain
IA [auth q]IPR034101Sm-like protein Lsm4Domain
IA [auth q]IPR010920LSM domain superfamilyHomologous Superfamily
JA [auth r]IPR001163Sm domain, eukaryotic/archaea-typeDomain
JA [auth r]IPR047575Sm domainDomain
JA [auth r]IPR033871Sm-like protein LSm5Domain
JA [auth r]IPR010920LSM domain superfamilyHomologous Superfamily
KA [auth s]IPR001163Sm domain, eukaryotic/archaea-typeDomain
KA [auth s]IPR047575Sm domainDomain
KA [auth s]IPR016487Sm-like protein Lsm6/SmFFamily
KA [auth s]IPR010920LSM domain superfamilyHomologous Superfamily
LA [auth t]IPR001163Sm domain, eukaryotic/archaea-typeDomain
LA [auth t]IPR047575Sm domainDomain
LA [auth t]IPR044641Sm-like protein Lsm7/SmGFamily
LA [auth t]IPR010920LSM domain superfamilyHomologous Superfamily
LA [auth t]IPR017132Sm-like protein Lsm7Family
NA [auth v]IPR016024Armadillo-type foldHomologous Superfamily
NA [auth v]IPR011989Armadillo-like helicalHomologous Superfamily
NA [auth v]IPR015016Splicing factor 3B subunit 1Domain
NA [auth v]IPR038737Splicing factor 3B subunit 1-likeFamily
OA [auth w]IPR018846Cleavage/polyadenylation specificity factor, A subunit, N-terminalDomain
OA [auth w]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
OA [auth w]IPR004871Cleavage/polyadenylation specificity factor, A subunit, C-terminalDomain
OA [auth w]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
PA [auth x]IPR017089Splicing factor 3B, subunit 5Family
PA [auth x]IPR009846Splicing factor 3B subunit 5/RDS3 complex subunit 10Family
QA [auth y]IPR005345PHF5-likeFamily
RA [auth z]IPR001611Leucine-rich repeatRepeat
RA [auth z]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
RA [auth z]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
SA [auth 1]IPR034562U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2Domain
SA [auth 1]IPR000504RNA recognition motif domainDomain
SA [auth 1]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
SA [auth 1]IPR035979RNA-binding domain superfamilyHomologous Superfamily
SA [auth 1]IPR034564U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1Domain
IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
IPR024936Cyclophilin-type peptidyl-prolyl cis-trans isomeraseFamily
IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
S [auth a],
TA [auth S],
Z [auth h]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
S [auth a],
TA [auth S],
Z [auth h]
IPR047575Sm domainDomain
S [auth a],
TA [auth S],
Z [auth h]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
S [auth a],
TA [auth S],
Z [auth h]
IPR010920LSM domain superfamilyHomologous Superfamily
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
BA [auth j],
U [auth c],
VA [auth U]
IPR027078Small nuclear ribonucleoprotein EFamily
BA [auth j],
U [auth c],
VA [auth U]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
BA [auth j],
U [auth c],
VA [auth U]
IPR047575Sm domainDomain
BA [auth j],
U [auth c],
VA [auth U]
IPR010920LSM domain superfamilyHomologous Superfamily
GA [auth o]IPR001163Sm domain, eukaryotic/archaea-typeDomain
GA [auth o]IPR047575Sm domainDomain
GA [auth o]IPR010920LSM domain superfamilyHomologous Superfamily
GA [auth o]IPR016654U6 snRNA-associated Sm-like protein LSm2Family
HA [auth p]IPR040002U6 snRNA-associated Sm-like protein Lsm3Family
HA [auth p]IPR001163Sm domain, eukaryotic/archaea-typeDomain
HA [auth p]IPR047575Sm domainDomain
HA [auth p]IPR010920LSM domain superfamilyHomologous Superfamily
HA [auth p]IPR034105Sm-like protein Lsm3Domain
IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
IPR041094Brr2, N-terminal helicase PWI domainDomain
IPR004179Sec63 domainDomain
IPR014756Immunoglobulin E-setHomologous Superfamily
IPR011545DEAD/DEAH box helicase domainDomain
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IPR001650Helicase, C-terminal domain-likeDomain
IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
IPR035892C2 domain superfamilyHomologous Superfamily
MA [auth u]IPR001163Sm domain, eukaryotic/archaea-typeDomain
MA [auth u]IPR047575Sm domainDomain
MA [auth u]IPR034103Sm-like protein Lsm8Domain
MA [auth u]IPR010920LSM domain superfamilyHomologous Superfamily
MA [auth u]IPR044642U6 snRNA-associated Sm-like protein Lsm1/8Family
IPR027104U4/U6 small nuclear ribonucleoprotein Prp3Family
IPR002483PWI domainDomain
IPR013881Pre-mRNA-splicing factor 3 domainDomain
IPR036483PWI domain superfamilyHomologous Superfamily
IPR010541Small nuclear ribonucleoprotein Prp3, C-terminal domainDomain
IPR042239Nop, C-terminal domainHomologous Superfamily
IPR019175Prp31 C-terminalDomain
IPR002687Nop domainDomain
IPR012976NOSICDomain
IPR027105U4/U6 small nuclear ribonucleoprotein Prp31Family
IPR036070Nop domain superfamilyHomologous Superfamily
IPR024767Pre-mRNA-splicing factor 38, C-terminalDomain
IPR005037Pre-mRNA-splicing factor 38Family

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ6P2Q9
PharosQ96DI7
PharosO43172
PharosO94906
PharosP83876
PharosP55081
PharosQ2TAY7
PharosQ96NC0
PharosP55769
PharosO43290
PharosO75554
PharosQ13123
AA [auth i],
T [auth b],
UA [auth T]
PharosP62306
CA [auth k],
V [auth d],
WA [auth V]
PharosP62308
DA [auth l],
W [auth e],
XA [auth W]
PharosP62318
EA [auth m],
X [auth f],
YA [auth X]
PharosP14678
FA [auth n],
Y [auth g],
ZA [auth Z]
PharosP62314
IA [auth q]PharosQ9Y4Z0
JA [auth r]PharosQ9Y4Y9
KA [auth s]PharosP62312
LA [auth t]PharosQ9UK45
NA [auth v]PharosO75533
OA [auth w]PharosQ15393
PA [auth x]PharosQ9BWJ5
QA [auth y]PharosQ7RTV0
SA [auth 1]PharosP08579
PharosO43447
S [auth a],
TA [auth S],
Z [auth h]
PharosP62316
PharosQ15029
BA [auth j],
U [auth c],
VA [auth U]
PharosP62304
GA [auth o]PharosQ9Y333
HA [auth p]PharosP62310
PharosO75643
MA [auth u]PharosO95777
PharosO43395
PharosQ8WWY3
PharosQ8NAV1