Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
M [auth K]SCOP2B SuperfamilyPre-mRNA-processing protein 45-like8092739 3002618 SCOP2B (2022-06-29)
JA [auth q]SCOP2B SuperfamilySm-like ribonucleoproteins8043703 3000419 SCOP2B (2022-06-29)
Y [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8043703 3000419 SCOP2B (2022-06-29)
O [auth M]SCOP2B SuperfamilyCCCH zinc finger-like8051791 3001741 SCOP2B (2022-06-29)
O [auth M]SCOP2B SuperfamilyRNA-binding domain RBD8051796 3000110 SCOP2B (2022-06-29)
EA [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8077613 3000419 SCOP2B (2022-06-29)
V [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8077613 3000419 SCOP2B (2022-06-29)
HA [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8098694 3000419 SCOP2B (2022-06-29)
W [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8098694 3000419 SCOP2B (2022-06-29)
KA [auth r]SCOP2B SuperfamilySm-like ribonucleoproteins8098668 3000419 SCOP2B (2022-06-29)
Z [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8098668 3000419 SCOP2B (2022-06-29)
BA [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8063490 3000419 SCOP2B (2022-06-29)
GA [auth m]SCOP2B SuperfamilySm-like ribonucleoproteins8063490 3000419 SCOP2B (2022-06-29)
DA [auth Y]SCOP2 FamilyCanonical RBD8073744 4000236 SCOP2 (2022-06-29)
DA [auth Y]SCOP2 SuperfamilyRNA-binding domain RBD8073745 3000110 SCOP2 (2022-06-29)
F [auth A]SCOP2B SuperfamilyRibonuclease H-like8040983 3000143 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
JA [auth q]LSMe5lj3q1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
Y [auth f]LSMe5lj3f1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
J [auth G]Isy1e5lj3G1 A: alpha bundlesX: Long alpha-hairpinH: ISY1 N-terminal domain-like (From Topology)T: ISY1 N-terminal domain-likeF: Isy1ECOD (1.6)
K [auth H]MIF4Ge5lj3H1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: MIF4GECOD (1.6)
K [auth H]MA3e5lj3H2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: MA3ECOD (1.6)
L [auth J]ANAPC4_WD40_9e5lj3J1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: ANAPC4_WD40_9ECOD (1.6)
N [auth L]G10e5lj3L1 A: few secondary structure elementsX: Pre-mRNA-splicing factor BUD31 (From Topology)H: Pre-mRNA-splicing factor BUD31 (From Topology)T: Pre-mRNA-splicing factor BUD31F: G10ECOD (1.6)
O [auth M]RRM_1_6e5lj3M2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_6ECOD (1.6)
O [auth M]Toruse5lj3M1 A: few secondary structure elementsX: CCCH zinc fingerH: CCCH zinc finger (From Topology)T: CCCH zinc fingerF: TorusECOD (1.6)
P [auth N]RRM_1_7e5lj3N1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_7ECOD (1.6)
P [auth N]KOG0153e5lj3N2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: KOG0153ECOD (1.6)
Q [auth O]Myb_DNA-binding_1e5lj3O1 A: alpha arraysX: HTHH: HTHT: tri-helicalF: Myb_DNA-binding_1ECOD (1.6)
S [auth R]cwf21e5lj3R1 A: alpha duplicates or obligate multimersX: cwf21 domain (From Topology)H: cwf21 domain (From Topology)T: cwf21 domainF: cwf21ECOD (1.6)
T [auth S]TPR_15e5lj3S1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_15ECOD (1.6)
U [auth T]Sufe5lj3T1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: SufECOD (1.6)
EA [auth k]LSMe5lj3k1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
V [auth b]LSMe5lj3b1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
HA [auth n]LSMe5lj3n1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
W [auth d]LSMe5lj3d1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
X [auth e]LSMe5lj3e1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
IA [auth p]LSMe5lj3p1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
KA [auth r]LSMe5lj3r1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
Z [auth g]LSMe5lj3g1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
AA [auth h]LSMe5lj3h1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
FA [auth l]LSMe5lj3l1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
BA [auth j]LSMe5lj3j1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
GA [auth m]LSMe5lj3m1 A: beta barrelsX: SH3H: SH3T: SH3F: LSMECOD (1.6)
CA [auth W]LRR_9e5lj3W1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Leucine-rich repeats (From Topology)T: Leucine-rich repeatsF: LRR_9ECOD (1.6)
DA [auth Y]RRM_1_2e5lj3Y1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: RRM_1_2ECOD (1.6)
F [auth A]U5_2-snRNA_bdge5lj3A3 A: alpha bundlesX: helical bundle domain in reverse transcriptase-like polymerases (From Topology)H: helical bundle domain in reverse transcriptase-like polymerases (From Topology)T: helical bundle domain in reverse transcriptase-like polymerasesF: U5_2-snRNA_bdgECOD (1.6)
F [auth A]PROCN_C,PROCN_Ne5lj3A1 A: alpha complex topologyX: Pre-mRNA-splicing factor 8 N-terminal domain (From Topology)H: Pre-mRNA-splicing factor 8 N-terminal domain (From Topology)T: Pre-mRNA-splicing factor 8 N-terminal domainF: PROCN_C,PROCN_NECOD (1.6)
F [auth A]RRM_4e5lj3A2 A: a+b two layersX: Alpha-beta plaitsH: Adenylyl and guanylyl cyclase catalytic domain-likeT: Adenylyl and guanylyl cyclase catalytic domain-likeF: RRM_4ECOD (1.6)
F [auth A]U6-snRNA_bdge5lj3A5 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: U6-snRNA_bdgECOD (1.6)
F [auth A]PRP8_domainIVe5lj3A4 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PRP8_domainIVECOD (1.6)
I [auth C]GTP_EFTU_D2_2e5lj3C5 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: GTP_EFTU_D2_2ECOD (1.6)
I [auth C]EFG_IVe5lj3C2 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: EFG_IVECOD (1.6)
I [auth C]EFG_Ce5lj3C4 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: EFG_CECOD (1.6)
I [auth C]EFG_IIe5lj3C3 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: EFG_IIECOD (1.6)
I [auth C]MnmE_helical_2nde5lj3C1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: MnmE_helical_2ndECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
JA [auth q]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Y [auth f]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
L [auth J]2.130.10.10 Mainly Beta 7 Propeller Methylamine Dehydrogenase Chain HCATH (4.3.0)
HA [auth n]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
W [auth d]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
X [auth e]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
IA [auth p]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
KA [auth r]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
Z [auth g]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
AA [auth h]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
FA [auth l]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
BA [auth j]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
GA [auth m]2.30.30.100 Mainly Beta Roll SH3 type barrels. CATH (4.3.0)
DA [auth Y]3.30.70.330 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits RRM (RNA recognition motif) domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
JA [auth q],
Y [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
J [auth G]PF06246Isy1-like splicing family (Isy1)Isy1-like splicing family- Family
L [auth J]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
N [auth L]PF01125Pre-mRNA-splicing factor BUD31 (BUD31)Pre-mRNA-splicing factor BUD31This entry includes Pre-mRNA-splicing factor BUD31, also known as G10 protein, and its homologues. BUD31 is involved in the pre-mRNA splicing process [1-3] and it is highly conserved in a wide range of eukaryotic species. Human BUD31 may play a role ...This entry includes Pre-mRNA-splicing factor BUD31, also known as G10 protein, and its homologues. BUD31 is involved in the pre-mRNA splicing process [1-3] and it is highly conserved in a wide range of eukaryotic species. Human BUD31 may play a role as a regulator of androgen receptor (AR) transcriptional activity, probably increasing the AR transcriptional activity [4].
Domain
O [auth M]PF16131Torus domain (Torus)Torus domainThis domain is found in pre-mRNA-splicing factor CWC2. It includes a CCCH-type zinc finger [1].Domain
O [auth M]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
P [auth N]PF21369STL11, N-terminal (STL11_N)STL11, N-terminalThis entry represents the N-terminal domain of STL11 from yeast and its homologues [1-4], such as RBM22 from human. This domain comprises a zinc finger, FYVE/PHD type. Members of this entry are involved in pre-mRNA splicing.Domain
Q [auth O]PF00249Myb-like DNA-binding domain (Myb_DNA-binding)Myb-like DNA-binding domainThis family contains the DNA binding domains from Myb proteins, as well as the SANT domain family [1].Domain
R [auth P]PF04889Cwf15/Cwc15 cell cycle control protein (Cwf_Cwc_15)Cwf15/Cwc15 cell cycle control protein- Family
S [auth R]PF08312cwf21 domain (cwf21)cwf21 domainThe cwf21 family is involved in mRNA splicing. It has been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe [1]. The function of the cwf21 domain is to bind directly to the spliceosomal protein Prp8. Mutations in the cwf21 dom ...The cwf21 family is involved in mRNA splicing. It has been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe [1]. The function of the cwf21 domain is to bind directly to the spliceosomal protein Prp8. Mutations in the cwf21 domain prevent Prp8 from binding [2]. The structure of this domain has recently been solved which shows this domain to be composed of two alpha helices.
Domain
T [auth S]PF02184HAT (Half-A-TPR) repeat (HAT)HAT (Half-A-TPR) repeat- Repeat
EA [auth k],
V [auth b]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
HA [auth n],
W [auth d]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
IA [auth p],
X [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
KA [auth r],
Z [auth g]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
AA [auth h],
FA [auth l]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
BA [auth j],
GA [auth m]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
CA [auth W]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
DA [auth Y]PF13893RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) (RRM_5)RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)The RRM motif 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 mo ...The RRM motif 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.
Domain
F [auth A]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
F [auth A]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
F [auth A]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
F [auth A]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
F [auth A]PF08083PROCN (NUC071) domain (PROCN)PROCN (NUC071) domainThe PROCN domain is the central domain in pre-mRNA splicing factors of PRO8 family [1].Domain
G [auth D]PF04502Saf4/Yju2 protein (Saf4_Yju2)Saf4/Yju2 protein- Family
H [auth F]PF10197N-terminal domain of CBF1 interacting co-repressor CIR (Cir_N)N-terminal domain of CBF1 interacting co-repressor CIRThis is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically ...This is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically to GTGGGAA motifs in responsive promoters, and it requires CIR as a co-repressor. CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex [1].
Domain
I [auth C]PF00679Elongation factor G C-terminus (EFG_C)Elongation factor G C-terminusThis domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.Domain
I [auth C]PF00009Elongation factor Tu GTP binding domain (GTP_EFTU)Elongation factor Tu GTP binding domainThis domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.Domain
I [auth C]PF16004116 kDa U5 small nuclear ribonucleoprotein component N-terminus (EFTUD2)116 kDa U5 small nuclear ribonucleoprotein component N-terminus- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
M [auth K]Pre-mRNA-processing protein 45-
JA [auth q],
Y [auth f]
Small nuclear ribonucleoprotein F
A [auth U]U5 snRNA (small nuclear RNA)---
J [auth G]ISY1-
K [auth H]CWC22---
L [auth J]PRP46-
N [auth L]Pre-mRNA-splicing factor BUD31-
O [auth M]CWC2
P [auth N]Pre-mRNA-splicing factor SLT11
Q [auth O]CEF1
R [auth P]CWC15
S [auth R]Pre-mRNA-splicing factor CWC21-
B [auth E]Exon 1 (5' exon) of UBC4 pre-mRNA---
T [auth S]CLF1
U [auth T]SYF1-
EA [auth k],
V [auth b]
Small nuclear ribonucleoprotein-associated protein B
HA [auth n],
W [auth d]
Small nuclear ribonucleoprotein Sm D3
IA [auth p],
X [auth e]
Small nuclear ribonucleoprotein E
KA [auth r],
Z [auth g]
Small nuclear ribonucleoprotein G
AA [auth h],
FA [auth l]
Small nuclear ribonucleoprotein Sm D1
BA [auth j],
GA [auth m]
Small nuclear ribonucleoprotein Sm D2
CA [auth W]U2 small nuclear ribonucleoprotein A'
C [auth I]Intron of UBC4 pre-mRNA---
DA [auth Y]U2 small nuclear ribonucleoprotein B''
LA [auth x]unknown---
D [auth Z]U2 snRNA (small nuclear RNA)---
E [auth V]U6 snRNA (small nuclear RNA)---
F [auth A]Pre-mRNA-splicing factor 8
G [auth D]Protein CWC16
H [auth F]Pre-mRNA-splicing factor CWC25-
I [auth C]Pre-mRNA-splicing factor SNU114

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
M [auth K]IPR017862SKI-interacting protein, SKIPFamily
M [auth K]IPR004015SKI-interacting protein SKIP, SNW domainDomain
JA [auth q],
Y [auth f]
IPR016487Sm-like protein Lsm6/SmFFamily
JA [auth q],
Y [auth f]
IPR034100Small nuclear ribonucleoprotein FFamily
JA [auth q],
Y [auth f]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
JA [auth q],
Y [auth f]
IPR047575Sm domainDomain
JA [auth q],
Y [auth f]
IPR010920LSM domain superfamilyHomologous Superfamily
J [auth G]IPR029012Helix hairpin bin domain superfamilyHomologous Superfamily
J [auth G]IPR009360Pre-mRNA-splicing factor Isy1Family
J [auth G]IPR037200Pre-mRNA-splicing factor Isy1 superfamilyHomologous Superfamily
L [auth J]IPR045241WD repeat Prp46/PLRG1-likeFamily
L [auth J]IPR001680WD40 repeatRepeat
L [auth J]IPR019775WD40 repeat, conserved siteConserved Site
L [auth J]IPR020472G-protein beta WD-40 repeatRepeat
L [auth J]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
L [auth J]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
N [auth L]IPR001748Pre-mRNA-splicing factor BUD31Family
N [auth L]IPR018230BUD31/G10-related, conserved siteConserved Site
O [auth M]IPR039171Pre-mRNA-splicing factor Cwc2/Slt11Family
O [auth M]IPR034181Pre-mRNA-splicing factor Cwc2, RNA recognition motifDomain
O [auth M]IPR000504RNA recognition motif domainDomain
O [auth M]IPR032297Torus domainDomain
O [auth M]IPR000571Zinc finger, CCCH-typeDomain
O [auth M]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
O [auth M]IPR035979RNA-binding domain superfamilyHomologous Superfamily
P [auth N]IPR039171Pre-mRNA-splicing factor Cwc2/Slt11Family
P [auth N]IPR034356Slt11, RNA recognition motifDomain
P [auth N]IPR048995STL11/RBM22-like, N-terminal domainDomain
Q [auth O]IPR047240Pre-mRNA splicing factor component CDC5L/Cef1, second SANT/myb-like domainDomain
Q [auth O]IPR017930Myb domainDomain
Q [auth O]IPR009057Homeobox-like domain superfamilyHomologous Superfamily
Q [auth O]IPR047242Pre-mRNA splicing factor component CDC5L/Cef1Family
Q [auth O]IPR001005SANT/Myb domainDomain
Q [auth O]IPR021786Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminalDomain
R [auth P]IPR006973Pre-mRNA-splicing factor Cwf15/Cwc15Family
S [auth R]IPR013170mRNA splicing factor Cwf21 domainDomain
T [auth S]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
T [auth S]IPR003107HAT (Half-A-TPR) repeatRepeat
T [auth S]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
U [auth T]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
U [auth T]IPR003107HAT (Half-A-TPR) repeatRepeat
U [auth T]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
EA [auth k],
V [auth b]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
EA [auth k],
V [auth b]
IPR047575Sm domainDomain
EA [auth k],
V [auth b]
IPR010920LSM domain superfamilyHomologous Superfamily
HA [auth n],
W [auth d]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
HA [auth n],
W [auth d]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
HA [auth n],
W [auth d]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
HA [auth n],
W [auth d]
IPR047575Sm domainDomain
HA [auth n],
W [auth d]
IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth p],
X [auth e]
IPR027078Small nuclear ribonucleoprotein EFamily
IA [auth p],
X [auth e]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
IA [auth p],
X [auth e]
IPR047575Sm domainDomain
IA [auth p],
X [auth e]
IPR010920LSM domain superfamilyHomologous Superfamily
KA [auth r],
Z [auth g]
IPR044641Sm-like protein Lsm7/SmGFamily
KA [auth r],
Z [auth g]
IPR034098Small nuclear ribonucleoprotein GFamily
KA [auth r],
Z [auth g]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
KA [auth r],
Z [auth g]
IPR047575Sm domainDomain
KA [auth r],
Z [auth g]
IPR010920LSM domain superfamilyHomologous Superfamily
AA [auth h],
FA [auth l]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
AA [auth h],
FA [auth l]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
AA [auth h],
FA [auth l]
IPR047575Sm domainDomain
AA [auth h],
FA [auth l]
IPR010920LSM domain superfamilyHomologous Superfamily
BA [auth j],
GA [auth m]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
BA [auth j],
GA [auth m]
IPR047575Sm domainDomain
BA [auth j],
GA [auth m]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
BA [auth j],
GA [auth m]
IPR010920LSM domain superfamilyHomologous Superfamily
CA [auth W]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
CA [auth W]IPR001611Leucine-rich repeatRepeat
CA [auth W]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
DA [auth Y]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
DA [auth Y]IPR000504RNA recognition motif domainDomain
DA [auth Y]IPR035979RNA-binding domain superfamilyHomologous Superfamily
F [auth A]IPR012984PROCT domainDomain
F [auth A]IPR012591PRO8NT domainDomain
F [auth A]IPR019580Pre-mRNA-processing-splicing factor 8, U6-snRNA-bindingDomain
F [auth A]IPR027652Pre-mRNA-processing-splicing factor 8Family
F [auth A]IPR043172Prp8 RNase domain IV, palm regionHomologous Superfamily
F [auth A]IPR012592PROCN domainDomain
F [auth A]IPR012337Ribonuclease H-like superfamilyHomologous Superfamily
F [auth A]IPR043173Prp8 RNase domain IV, fingers regionHomologous Superfamily
F [auth A]IPR021983PRP8 domain IV coreDomain
F [auth A]IPR019581Pre-mRNA-processing-splicing factor 8, U5-snRNA-bindingDomain
F [auth A]IPR037518MPN domainDomain
F [auth A]IPR019582RNA recognition motif, spliceosomal PrP8Domain
F [auth A]IPR042516Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamilyHomologous Superfamily
F [auth A]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
G [auth D]IPR043701Splicing factor Yju2Family
G [auth D]IPR007590Saf4/Yju2 proteinFamily
H [auth F]IPR019339CBF1-interacting co-repressor CIR, N-terminal domainDomain
H [auth F]IPR022209Pre-mRNA splicing factorFamily
I [auth C]IPR005517Translation elongation factor EFG/EF2, domain IVDomain
I [auth C]IPR000795Translational (tr)-type GTP-binding domainDomain
I [auth C]IPR035647EF-G domain III/V-likeHomologous Superfamily
I [auth C]IPR035655116kDa U5 small nuclear ribonucleoprotein component, C-terminalDomain
I [auth C]IPR009000Translation protein, beta-barrel domain superfamilyHomologous Superfamily
I [auth C]IPR020568Ribosomal protein uS5 domain 2-type superfamilyHomologous Superfamily
I [auth C]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
I [auth C]IPR014721Small ribosomal subunit protein uS5 domain 2-type fold, subgroupHomologous Superfamily
I [auth C]IPR031950116kDa U5 small nuclear ribonucleoprotein component, N-terminalDomain
I [auth C]IPR000640Elongation factor EFG, domain V-likeDomain
I [auth C]IPR044121Snu114, GTP-binding domainDomain