Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
B [auth E]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
B [auth E]SCOP2B SuperfamilyWD40 repeat-like8052534 3001694 SCOP2B (2022-06-29)
B [auth E]SCOP2B SuperfamilyWD40 repeat-like8052535 3001694 SCOP2B (2022-06-29)
B [auth E]SCOP2B SuperfamilyWD40 repeat-like8051197 3001694 SCOP2B (2022-06-29)
C [auth b]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
HA [auth i]SCOP2B SuperfamilySm-like ribonucleoproteins8063452 3000419 SCOP2B (2022-06-29)
D [auth W]SCOP2B SuperfamilyL domain-like8043993 3001010 SCOP2B (2022-06-29)
E [auth w]SCOP2B SuperfamilyRNA-binding domain RBD8090834 3000110 SCOP2B (2022-06-29)
NA [auth k]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
F [auth d]SCOP2B SuperfamilySm-like ribonucleoproteins8063468 3000419 SCOP2B (2022-06-29)
G [auth U]SCOP2B SuperfamilyARM repeat-like8090869 3000116 SCOP2B (2022-06-29)
G [auth U]SCOP2B SuperfamilyUpf1 beta-barrel domain-like8090870 3002168 SCOP2B (2022-06-29)
G [auth U]SCOP2B SuperfamilyRecA-like P-loop NTPases8090871 3002019 SCOP2B (2022-06-29)
G [auth U]SCOP2B SuperfamilyRecA-like P-loop NTPases8090872 3002019 SCOP2B (2022-06-29)
J [auth B]SCOP2B SuperfamilyRNA-binding domain RBD8035327 3000110 SCOP2B (2022-06-29)
K [auth z]SCOP2B SuperfamilyRNA-binding domain RBD8040695 3000110 SCOP2B (2022-06-29)
L [auth q]SCOP2B SuperfamilyUbiquitin-like8038047 3000157 SCOP2B (2022-06-29)
M [auth s]SCOP2B SuperfamilyE set domains8055093 3000070 SCOP2B (2022-06-29)
M [auth s]SCOP2B SuperfamilyBrl domain-like8036193 3000115 SCOP2B (2022-06-29)
P [auth 0]SCOP2B SuperfamilySMAD/FHA domain-like8100246 3000137 SCOP2B (2022-06-29)
R [auth 1]SCOP2B SuperfamilyRNA-binding domain RBD8061967 3000110 SCOP2B (2022-06-29)
S [auth L]SCOP2B SuperfamilyHomeodomain-like8089608 3000001 SCOP2B (2022-06-29)
X [auth Y]SCOP2B SuperfamilyPWI domain8036462 3000964 SCOP2B (2022-06-29)
Y [auth 7]SCOP2B SuperfamilyWinged helix DNA-binding domain8052331 3000034 SCOP2B (2022-06-29)
CA [auth y]SCOP2B SuperfamilyTriquetra zinc finger motif8051848 3002040 SCOP2B (2022-06-29)
FA [auth h]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
ZA [auth a]SCOP2B SuperfamilySm-like ribonucleoproteins8041749 3000419 SCOP2B (2022-06-29)
IA [auth t]SCOP2B SuperfamilyCyclophilin-like8035793 3000168 SCOP2B (2022-06-29)
JA [auth m]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
VA [auth f]SCOP2B SuperfamilySm-like ribonucleoproteins8041747 3000419 SCOP2B (2022-06-29)
LA [auth l]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
BB [auth e]SCOP2B SuperfamilySm-like ribonucleoproteins8041751 3000419 SCOP2B (2022-06-29)
MA [auth A]SCOP2B SuperfamilyJAB1/MPN domain-like8053277 3001105 SCOP2B (2022-06-29)
MA [auth A]SCOP2B SuperfamilyRibonuclease H-like8041105 3000143 SCOP2B (2022-06-29)
PA [auth j]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
DB [auth c]SCOP2B SuperfamilySm-like ribonucleoproteins8063476 3000419 SCOP2B (2022-06-29)
XA [auth g]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
RA [auth n]SCOP2B SuperfamilySm-like ribonucleoproteins8041748 3000419 SCOP2B (2022-06-29)
SA [auth P]SCOP2B SuperfamilyRNA-binding domain RBD8064957 3000110 SCOP2B (2022-06-29)
UA [auth p]SCOP2B SuperfamilySurp module (SWAP domain)8033803 3001401 SCOP2B (2022-06-29)
GA [auth o]SCOP2B SuperfamilyRNA-binding domain RBD8039202 3000110 SCOP2B (2022-06-29)
GA [auth o]SCOP2B SuperfamilyCyclophilin-like8035984 3000168 SCOP2B (2022-06-29)
QA [auth I]SCOP2B SuperfamilyPRP38-like8055808 3002318 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth D]PF00400e7abiD1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
B [auth E]PF03178,PF10433e7abiE3 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF03178,PF10433ECOD (1.6)
B [auth E]PF10433e7abiE2 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF10433ECOD (1.6)
B [auth E]PF03178e7abiE1 A: alpha arraysX: HTHH: HTHT: tri-helicalF: PF03178ECOD (1.6)
C [auth b]PF01423e7abib1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
HA [auth i]PF01423e7abii1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
D [auth W]PF14580e7abiW1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Leucine-rich repeats (From Topology)T: Leucine-rich repeatsF: PF14580ECOD (1.6)
E [auth w]PF00076e7abiw1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
NA [auth k]PF01423e7abik1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
F [auth d]PF01423e7abid1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
G [auth U]PF21143e7abiU5 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF21143ECOD (1.6)
G [auth U]PF16399e7abiU3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF16399ECOD (1.6)
G [auth U]PF21144e7abiU2 A: a+b two layersX: Spliceosomal helicase Aquarius insert domain (From Topology)H: Spliceosomal helicase Aquarius insert domain (From Topology)T: Spliceosomal helicase Aquarius insert domainF: PF21144ECOD (1.6)
G [auth U]PF13086e7abiU4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF13086ECOD (1.6)
G [auth U]PF13087e7abiU1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF13087ECOD (1.6)
H [auth x]PF07189e7abix1 A: alpha arraysX: RDS3 complex subunit 10 (From Topology)H: RDS3 complex subunit 10 (From Topology)T: RDS3 complex subunit 10F: PF07189ECOD (1.6)
J [auth B]PF00076e7abiB1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
K [auth z]PF00076e7abiz1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
L [auth q]PF00240e7abiq1 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: PF00240ECOD (1.6)
M [auth s]PF02889e7abis9 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Immunoglobulin/Fibronectin type III/E set domains/PapD-likeF: PF02889ECOD (1.6)
M [auth s]F_UNCLASSIFIEDe7abis10 A: alpha arraysX: HTHH: HTHT: wingedF: F_UNCLASSIFIEDECOD (1.6)
M [auth s]F_UNCLASSIFIEDe7abis7 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)
M [auth s]PF02889e7abis3 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)
M [auth s]PF00270e7abis11 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00270ECOD (1.6)
M [auth s]PF00271e7abis5 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00271ECOD (1.6)
P [auth 0]PF00498e7abi01 A: beta sandwichesX: SMAD/FHA domain (From Topology)H: SMAD/FHA domain (From Topology)T: SMAD/FHA domainF: PF00498ECOD (1.6)
QPF01125e7abiQ1 A: few secondary structure elementsX: Pre-mRNA-splicing factor BUD31 (From Topology)H: Pre-mRNA-splicing factor BUD31 (From Topology)T: Pre-mRNA-splicing factor BUD31F: PF01125ECOD (1.6)
R [auth 1]PF00076e7abi11 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
S [auth L]PF00249e7abiL2 A: alpha arraysX: HTHH: HTHT: tri-helicalF: PF00249ECOD (1.6)
T [auth N]PF12171e7abiN1 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)
U [auth S]PF08216e7abiS1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF08216ECOD (1.6)
V [auth r]PF03144e7abir2 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: PF03144ECOD (1.6)
V [auth r]PF03764e7abir3 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)
V [auth r]PF00679e7abir1 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)
V [auth r]PF14492e7abir4 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)
V [auth r]PF00009,PF16004e7abir5 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00009,PF16004ECOD (1.6)
X [auth Y]PF01480e7abiY1 A: alpha arraysX: PWI domain-likeH: PWI domain (From Topology)T: PWI domainF: PF01480ECOD (1.6)
Y [auth 7]PF18131e7abi71 A: beta barrelsX: SH3H: SH3T: SH3F: PF18131ECOD (1.6)
Y [auth 7]PF10357e7abi72 A: alpha arraysX: HTHH: HTHT: wingedF: PF10357ECOD (1.6)
Z [auth M]F_UNCLASSIFIEDe7abiM1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
BA [auth O]PF02184e7abiO1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF02184ECOD (1.6)
CA [auth y]PF03660e7abiy1 A: few secondary structure elementsX: Glucocorticoid receptor-likeH: LIM domain-likeT: PHD finger-like domain-containing protein 5AF: PF03660ECOD (1.6)
EA [auth G]PF00400e7abiG1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
FA [auth h]PF01423e7abih1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
ZA [auth a]PF01423e7abia1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
IA [auth t]PF00160e7abit1 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: PF00160ECOD (1.6)
IA [auth t]F_UNCLASSIFIEDe7abit2 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: F_UNCLASSIFIEDECOD (1.6)
IA [auth t]F_UNCLASSIFIEDe7abit3 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: RING/U-boxF: F_UNCLASSIFIEDECOD (1.6)
JA [auth m]PF01423e7abim1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
VA [auth f]PF01423e7abif1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
LA [auth l]PF01423e7abil1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
BB [auth e]PF01423e7abie1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
MA [auth A]PF10596,PF10597e7abiA4 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)
MA [auth A]PF08082,PF08083e7abiA2 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)
MA [auth A]PF10598e7abiA6 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)
MA [auth A]PF01398,PF08084e7abiA3 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398,PF08084ECOD (1.6)
MA [auth A]PF10596e7abiA1 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF10596ECOD (1.6)
MA [auth A]PF12134e7abiA5 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF12134ECOD (1.6)
PA [auth j]PF01423e7abij1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
DB [auth c]PF01423e7abic1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
XA [auth g]PF01423e7abig1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
RA [auth n]PF01423e7abin1 A: beta barrelsX: SH3H: SH3T: SH3F: PF01423ECOD (1.6)
SA [auth P]PF00076e7abiP3 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
SA [auth P]PF21369e7abiP1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF21369ECOD (1.6)
SA [auth P]PF18345e7abiP2 A: few secondary structure elementsX: CCCH zinc fingerH: CCCH zinc finger (From Topology)T: CCCH zinc fingerF: PF18345ECOD (1.6)
UA [auth p]PF01805e7abip2 A: alpha bundlesX: Surp module (SWAP domain) (From Topology)H: Surp module (SWAP domain) (From Topology)T: Surp module (SWAP domain)F: PF01805ECOD (1.6)
WA [auth F]PF16835e7abiF2 A: beta sandwichesX: HSP20-likeH: Pre-mRNA-splicing factor PRP11 C-terminal domain (From Topology)T: Pre-mRNA-splicing factor PRP11 C-terminal domainF: PF16835ECOD (1.6)
WA [auth F]PF12874e7abiF1 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF12874ECOD (1.6)
AB [auth u]PF08920,PF22646e7abiu1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF08920,PF22646ECOD (1.6)
GA [auth o]PF00160e7abio2 A: beta barrelsX: Cyclophilin-like (From Topology)H: Cyclophilin-like (From Topology)T: Cyclophilin-likeF: PF00160ECOD (1.6)
GA [auth o]PF00076e7abio1 A: a+b two layersX: Alpha-beta plaitsH: RNA-binding domain, RBD (From Topology)T: RNA-binding domain, RBDF: PF00076ECOD (1.6)
QA [auth I]PF03371e7abiI1 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
A [auth D]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
B [auth E]PF10433Mono-functional DNA-alkylating methyl methanesulfonate N-term (MMS1_N)Mono-functional DNA-alkylating methyl methanesulfonate N-term- Repeat
B [auth E]PF03178CPSF A subunit region (CPSF_A)CPSF A subunit region- Repeat
C [auth b],
HA [auth i]
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
D [auth W]PF14580Leucine-rich repeat (LRR_9)Leucine-rich repeat- Repeat
E [auth w]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
F [auth d],
NA [auth k]
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
G [auth U]PF21144Intron-binding protein aquarius insert domain (Aquarius_N_3rd)Intron-binding protein aquarius insert domainThis entry represents the insert domain of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly [1,2].Domain
G [auth U]PF21143Intron-binding protein aquarius, beta-barrel (Aquarius_N_2nd)Intron-binding protein aquarius, beta-barrelThis entry represents the beta-barrel domain found at the N-terminal of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly [1,2].Domain
G [auth U]PF13086AAA domain (AAA_11)AAA domainThis family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.Domain
G [auth U]PF13087AAA domain (AAA_12)AAA domainThis family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.Domain
G [auth U]PF16399Intron-binding protein aquarius N-terminal (Aquarius_N_1st)Intron-binding protein aquarius N-terminal- Repeat
H [auth x]PF07189Splicing factor 3B subunit 10 (SF3b10) (SF3b10)Splicing factor 3B subunit 10 (SF3b10)- Family
J [auth B]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
K [auth z]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
L [auth q]PF00240Ubiquitin family (ubiquitin)Ubiquitin familyThis family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry ...This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].
Domain
M [auth s]PF02889Sec63 Brl domain (Sec63)Sec63 Brl domain- Family
M [auth s]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
M [auth s]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
O [auth 3]PF09736Pre-mRNA-splicing factor of RES complex (Bud13)Pre-mRNA-splicing factor of RES complex- Family
P [auth 0]PF00498FHA domain (FHA)FHA domain- Family
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
R [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
S [auth L]PF13921Myb-like DNA-binding domain (Myb_DNA-bind_6)Myb-like DNA-binding domainThis family contains the DNA binding domains from Myb proteins, as well as the SANT domain family [1].Domain
T [auth N]PF12171Zinc-finger double-stranded RNA-binding (zf-C2H2_jaz)Zinc-finger double-stranded RNA-binding- Family
U [auth S]PF08216Catenin-beta-like, Arm-motif containing nuclear (CTNNBL)Catenin-beta-like, Arm-motif containing nuclear- Repeat
V [auth r]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
V [auth r]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
V [auth r]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
V [auth r]PF16004116 kDa U5 small nuclear ribonucleoprotein component N-terminus (EFTUD2)116 kDa U5 small nuclear ribonucleoprotein component N-terminus- Family
V [auth r]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
V [auth r]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
W [auth R]PF04889Cwf15/Cwc15 cell cycle control protein (Cwf_Cwc_15)Cwf15/Cwc15 cell cycle control protein- Family
X [auth Y]PF01480PWI domain (PWI)PWI domain- Family
Y [auth 7]PF18131KN17 SH3-like C-terminal domain (KN17_SH3)KN17 SH3-like C-terminal domainThis domain can be found at the C terminus of the human KIN17 protein and its homologues. In human cells, over-expression of KIN17 modifies the nuclear morphology and inhibits S-phase progression, thus blocking cell growth as part of the response t ...This domain can be found at the C terminus of the human KIN17 protein and its homologues. In human cells, over-expression of KIN17 modifies the nuclear morphology and inhibits S-phase progression, thus blocking cell growth as part of the response to genotoxics. The C-terminal domain exhibits an all-beta structure consisting of two tightly packed SH3-like subdomains. It binds to RNA and is generally well conserved. This domain has structural similarity with various SH3-like domains, although it lacks similarities in both primary sequence and charge distribution [1].
Domain
Y [auth 7]PF10357Domain of Kin17 curved DNA-binding protein (Kin17_mid)Domain of Kin17 curved DNA-binding protein- Family
Z [auth M]PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
AA [auth K]PF06991Microfibril-associated/Pre-mRNA processing (MFAP1)Microfibril-associated/Pre-mRNA processing- Family
BA [auth O]PF02184HAT (Half-A-TPR) repeat (HAT)HAT (Half-A-TPR) repeat- Repeat
CA [auth y]PF03660PHF5-like protein (PHF5)PHF5-like protein- Family
EA [auth G]PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
FA [auth h],
ZA [auth a]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
IA [auth t]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
JA [auth m],
VA [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
BB [auth e],
LA [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
MA [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
MA [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
MA [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
MA [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
MA [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
MA [auth A]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
MA [auth A]PF08084PROCT (NUC072) domain (PROCT)PROCT (NUC072) domainThe PROCT domain is the C-terminal domain in pre-mRNA splicing factors of PRO8 family [1].Domain
DB [auth c],
PA [auth j]
PF01423LSM domain (LSM)LSM domainThe LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) i ...The LSM domain contains Sm proteins as well as other related LSM (Like Sm) proteins. The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B', D1, D2, D3, E, F and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs. The U6 snRNP binds to the LSM (Like Sm) proteins [3]. Sm proteins are also found in archaebacteria, which do not have any splicing apparatus suggesting a more general role for Sm proteins. All Sm proteins contain a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. This family also includes the bacterial Hfq (host factor Q) proteins. Hfq are also RNA-binding proteins, that form hexameric rings.
Domain
RA [auth n],
XA [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
SA [auth P]PF00076RNA recognition motif (RRM_1)RNA recognition motifThe RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and pro ...The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.
Domain
UA [auth p]PF01805Surp module (Surp)Surp module- Family
WA [auth F]PF12874Zinc-finger of C2H2 type (zf-met)Zinc-finger of C2H2 typeThis is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.Domain
YA [auth 4]PF16837Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9 (SF3A3)Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9SF3A3 is one of the components of the SF3a splicing factor complex of the mature U2 snRNP (small nuclear ribonucleoprotein particle). In yeast, SF3a shows a bifurcated assembly structure of three subunits, Prp9 (subunit 3), Prp11 (subunit 2) and Prp2 ...SF3A3 is one of the components of the SF3a splicing factor complex of the mature U2 snRNP (small nuclear ribonucleoprotein particle). In yeast, SF3a shows a bifurcated assembly structure of three subunits, Prp9 (subunit 3), Prp11 (subunit 2) and Prp21 (subunit 1). Prp9 and Prp21 were not thought to interact with each other but the alpha1 helix of Prp9 does make important contacts with the SURP2 domain of Prp21, thus the two do interact via a bidentate-binding mode. Prp9 harbours a major binding site for stem-loop IIa of U2 snRNA [1].
Domain
YA [auth 4]PF13297Replication stress response SDE2 C-terminal (SDE2_2C)Replication stress response SDE2 C-terminalThis domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved fr ...This domain represents the C-terminal region of the Replication stress response SDE2, a genome surveillance factor. It contains the DNA-binding SAP domain, frequently found in proteins involved in DNA repair. SDE2 C-terminal domain must be cleaved from its N-terminal at a diglycine motif within the ubiquitin-like fold, after Proliferating cell nuclear antigen (PCNA) interaction. This generates a functional protein that negatively regulates damage-inducible PCNA monoubiquitination, which then is proteolytically degraded to allow S phase progression and replication fork recovery in response to DNA damage [1].
Domain
YA [auth 4]PF12108Splicing factor SF3a60 binding domain (SF3a60_bindingd)Splicing factor SF3a60 binding domainThis domain is found in eukaryotes. This domain is about 30 amino acids in length. This domain has a single completely conserved residue Y that may be functionally important. SF3a60 makes up the SF3a complex with SF3a66 and SF3a120. This domain is th ...This domain is found in eukaryotes. This domain is about 30 amino acids in length. This domain has a single completely conserved residue Y that may be functionally important. SF3a60 makes up the SF3a complex with SF3a66 and SF3a120. This domain is the binding site of SF3a60 for SF3a120. The SF3a complex is part of the spliceosome, a protein complex involved in splicing mRNA after transcription.
Domain
GA [auth o]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
GA [auth o]PF00076RNA recognition motif (RRM_1)RNA recognition motifThe RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and pro ...The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.
Domain
QA [auth I]PF03371PRP38 family (PRP38)PRP38 family- Family
CB [auth T]PF04037Domain of unknown function (DUF382) (DUF382)Domain of unknown function (DUF382)- Family
CB [auth T]PF04046PSP (PSP)PSP- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth D]U5 small nuclear ribonucleoprotein 40 kDa protein
B [auth E]Splicing factor 3B subunit 3
C [auth b],
HA [auth i]
Small nuclear ribonucleoprotein F
D [auth W]U2 small nuclear ribonucleoprotein A'
E [auth w]Splicing factor 3B subunit 4
F [auth d],
NA [auth k]
Small nuclear ribonucleoprotein G
G [auth U]Intron-binding protein aquarius
H [auth x]Splicing factor 3B subunit 5
I [auth 6]U6 snRNA---
J [auth B]U2 small nuclear ribonucleoprotein B''
K [auth z]Splicing factor 3B subunit 6
L [auth q]Ubiquitin-like protein 5
M [auth s]U5 small nuclear ribonucleoprotein 200 kDa helicase
N [auth v]SNW domain-containing protein 1
O [auth 3]BUD13 homolog
P [auth 0]Smad nuclear-interacting protein 1
Protein BUD31 homolog
R [auth 1]RNA-binding motif protein, X-linked 2
S [auth L]Cell division cycle 5-like protein
T [auth N]Zinc finger matrin-type protein 2
U [auth S]Beta-catenin-like protein 1
V [auth r]116 kDa U5 small nuclear ribonucleoprotein component
W [auth R]Spliceosome-associated protein CWC15 homolog
X [auth Y]Serine/arginine repetitive matrix protein 1
Y [auth 7]DNA/RNA-binding protein KIN17
Z [auth M]Pre-mRNA-splicing factor SYF1-
AA [auth K]Microfibrillar-associated protein 1
BA [auth O]Crooked neck-like protein 1
CA [auth y]PHD finger-like domain-containing protein 5A
DA [auth 2]U2 snRNA---
EA [auth G]Pleiotropic regulator 1-
FA [auth h],
ZA [auth a]
Small nuclear ribonucleoprotein Sm D2
IA [auth t]RING-type E3 ubiquitin-protein ligase PPIL2
JA [auth m],
VA [auth f]
Small nuclear ribonucleoprotein-associated proteins B and B'
KA [auth Z]MINX M3 pre-mRNA---
BB [auth e],
LA [auth l]
Small nuclear ribonucleoprotein Sm D3
MA [auth A]Pre-mRNA-processing-splicing factor 8
OA [auth 8]Pre-mRNA-processing factor 17
DB [auth c],
PA [auth j]
Small nuclear ribonucleoprotein E
RA [auth n],
XA [auth g]
Small nuclear ribonucleoprotein Sm D1
SA [auth P]Pre-mRNA-splicing factor RBM22
TA [auth 5]U5 snRNA---
UA [auth p]Splicing factor 3A subunit 1
WA [auth F]Splicing factor 3A subunit 2
YA [auth 4]Splicing factor 3A subunit 3
AB [auth u]Splicing factor 3B subunit 1
GA [auth o]Peptidyl-prolyl cis-trans isomerase E
QA [auth I]Pre-mRNA-splicing factor 38A
CB [auth T]Splicing factor 3B subunit 2

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A [auth D]IPR019775WD40 repeat, conserved siteConserved Site
A [auth D]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
A [auth D]IPR001680WD40 repeatRepeat
A [auth D]IPR020472G-protein beta WD-40 repeatRepeat
A [auth D]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
B [auth E]IPR018846Cleavage/polyadenylation specificity factor, A subunit, N-terminalDomain
B [auth E]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
B [auth E]IPR004871Cleavage/polyadenylation specificity factor, A subunit, C-terminalDomain
B [auth E]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
C [auth b],
HA [auth i]
IPR016487Sm-like protein Lsm6/SmFFamily
C [auth b],
HA [auth i]
IPR034100Small nuclear ribonucleoprotein FFamily
C [auth b],
HA [auth i]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
C [auth b],
HA [auth i]
IPR047575Sm domainDomain
C [auth b],
HA [auth i]
IPR010920LSM domain superfamilyHomologous Superfamily
D [auth W]IPR001611Leucine-rich repeatRepeat
D [auth W]IPR003603U2A'/phosphoprotein 32 family A, C-terminalDomain
D [auth W]IPR032675Leucine-rich repeat domain superfamilyHomologous Superfamily
E [auth w]IPR034159SF3B4, RNA recognition motif 2Domain
E [auth w]IPR000504RNA recognition motif domainDomain
E [auth w]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
E [auth w]IPR035979RNA-binding domain superfamilyHomologous Superfamily
E [auth w]IPR034158SF3B4, RNA recognition motif 1Domain
F [auth d],
NA [auth k]
IPR044641Sm-like protein Lsm7/SmGFamily
F [auth d],
NA [auth k]
IPR034098Small nuclear ribonucleoprotein GFamily
F [auth d],
NA [auth k]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
F [auth d],
NA [auth k]
IPR047575Sm domainDomain
F [auth d],
NA [auth k]
IPR010920LSM domain superfamilyHomologous Superfamily
G [auth U]IPR048966RNA helicase aquarius, beta-barrelDomain
G [auth U]IPR048967RNA helicase aquarius, insertion domainDomain
G [auth U]IPR041677DNA2/NAM7 helicase, helicase domainDomain
G [auth U]IPR026300CWF11 familyFamily
G [auth U]IPR045055DNA2/NAM7-like helicaseFamily
G [auth U]IPR032174RNA helicase aquarius, N-terminal domainDomain
G [auth U]IPR041679DNA2/NAM7 helicase-like, C-terminalDomain
G [auth U]IPR047187Upf1-like, C-terminal helicase domainDomain
G [auth U]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
H [auth x]IPR017089Splicing factor 3B, subunit 5Family
H [auth x]IPR009846Splicing factor 3B subunit 5/RDS3 complex subunit 10Family
J [auth B]IPR034562U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2Domain
J [auth B]IPR000504RNA recognition motif domainDomain
J [auth B]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
J [auth B]IPR035979RNA-binding domain superfamilyHomologous Superfamily
J [auth B]IPR034564U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1Domain
K [auth z]IPR000504RNA recognition motif domainDomain
K [auth z]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
K [auth z]IPR034150SF3B6, RNA recognition motifDomain
K [auth z]IPR035979RNA-binding domain superfamilyHomologous Superfamily
L [auth q]IPR039732Ubiquitin-like modifier Hub1/Ubl5Family
L [auth q]IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
L [auth q]IPR000626Ubiquitin-like domainDomain
M [auth s]IPR048863Pre-mRNA-splicing helicase BRR2-like, plug domainDomain
M [auth s]IPR041094Brr2, N-terminal helicase PWI domainDomain
M [auth s]IPR004179Sec63 domainDomain
M [auth s]IPR014756Immunoglobulin E-setHomologous Superfamily
M [auth s]IPR011545DEAD/DEAH box helicase domainDomain
M [auth s]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
M [auth s]IPR001650Helicase, C-terminal domain-likeDomain
M [auth s]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
M [auth s]IPR014001Helicase superfamily 1/2, ATP-binding domainDomain
M [auth s]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
M [auth s]IPR035892C2 domain superfamilyHomologous Superfamily
N [auth v]IPR017862SKI-interacting protein, SKIPFamily
N [auth v]IPR004015SKI-interacting protein SKIP, SNW domainDomain
O [auth 3]IPR018609Bud13Family
P [auth 0]IPR008984SMAD/FHA domain superfamilyHomologous Superfamily
P [auth 0]IPR000253Forkhead-associated (FHA) domainDomain
IPR001748Pre-mRNA-splicing factor BUD31Family
IPR018230BUD31/G10-related, conserved siteConserved Site
R [auth 1]IPR000504RNA recognition motif domainDomain
R [auth 1]IPR045844Ist3-like, RNA recognition motifDomain
R [auth 1]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
R [auth 1]IPR035979RNA-binding domain superfamilyHomologous Superfamily
S [auth L]IPR047240Pre-mRNA splicing factor component CDC5L/Cef1, second SANT/myb-like domainDomain
S [auth L]IPR017930Myb domainDomain
S [auth L]IPR009057Homeobox-like domain superfamilyHomologous Superfamily
S [auth L]IPR047242Pre-mRNA splicing factor component CDC5L/Cef1Family
S [auth L]IPR001005SANT/Myb domainDomain
S [auth L]IPR021786Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminalDomain
T [auth N]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
T [auth N]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
T [auth N]IPR040107U4/U6.U5 small nuclear ribonucleoprotein component Snu23Family
T [auth N]IPR022755Zinc finger, double-stranded RNA bindingDomain
U [auth S]IPR016024Armadillo-type foldHomologous Superfamily
U [auth S]IPR039678Beta-catenin-like protein 1Family
U [auth S]IPR011989Armadillo-like helicalHomologous Superfamily
U [auth S]IPR013180Beta-catenin-like protein 1, N-terminalDomain
V [auth r]IPR005517Translation elongation factor EFG/EF2, domain IVDomain
V [auth r]IPR000795Translational (tr)-type GTP-binding domainDomain
V [auth r]IPR035647EF-G domain III/V-likeHomologous Superfamily
V [auth r]IPR035655116kDa U5 small nuclear ribonucleoprotein component, C-terminalDomain
V [auth r]IPR041095Elongation Factor G, domain IIDomain
V [auth r]IPR004161Translation elongation factor EFTu-like, domain 2Domain
V [auth r]IPR009000Translation protein, beta-barrel domain superfamilyHomologous Superfamily
V [auth r]IPR020568Ribosomal protein uS5 domain 2-type superfamilyHomologous Superfamily
V [auth r]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
V [auth r]IPR014721Small ribosomal subunit protein uS5 domain 2-type fold, subgroupHomologous Superfamily
V [auth r]IPR031950116kDa U5 small nuclear ribonucleoprotein component, N-terminalDomain
V [auth r]IPR000640Elongation factor EFG, domain V-likeDomain
V [auth r]IPR044121Snu114, GTP-binding domainDomain
V [auth r]IPR005225Small GTP-binding protein domainDomain
W [auth R]IPR006973Pre-mRNA-splicing factor Cwf15/Cwc15Family
X [auth Y]IPR002483PWI domainDomain
X [auth Y]IPR036483PWI domain superfamilyHomologous Superfamily
Y [auth 7]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
Y [auth 7]IPR019447DNA/RNA-binding protein Kin17, WH-like domainDomain
Y [auth 7]IPR014722Large ribosomal subunit protein uL2, domain 2Homologous Superfamily
Y [auth 7]IPR041995Kin17, KOW domainDomain
Y [auth 7]IPR041330KN17, SH3-like C-terminal domainDomain
Y [auth 7]IPR037321KIN17-like proteinFamily
Y [auth 7]IPR038254DNA/RNA-binding protein KIN17, WH-like domain superfamilyHomologous Superfamily
Z [auth M]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
Z [auth M]IPR003107HAT (Half-A-TPR) repeatRepeat
Z [auth M]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
Z [auth M]IPR019734Tetratricopeptide repeatRepeat
AA [auth K]IPR033194Microfibrillar-associated protein 1Family
AA [auth K]IPR009730Micro-fibrillar-associated protein 1, C-terminalDomain
BA [auth O]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
BA [auth O]IPR003107HAT (Half-A-TPR) repeatRepeat
BA [auth O]IPR045075Pre-mRNA-splicing factor Syf1-likeFamily
CA [auth y]IPR005345PHF5-likeFamily
EA [auth G]IPR019775WD40 repeat, conserved siteConserved Site
EA [auth G]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
EA [auth G]IPR045241WD repeat Prp46/PLRG1-likeFamily
EA [auth G]IPR001680WD40 repeatRepeat
EA [auth G]IPR020472G-protein beta WD-40 repeatRepeat
EA [auth G]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
FA [auth h],
ZA [auth a]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
FA [auth h],
ZA [auth a]
IPR047575Sm domainDomain
FA [auth h],
ZA [auth a]
IPR027248Small nuclear ribonucleoprotein Sm D2Family
FA [auth h],
ZA [auth a]
IPR010920LSM domain superfamilyHomologous Superfamily
IA [auth t]IPR003613U-box domainDomain
IA [auth t]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
IA [auth t]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
IA [auth t]IPR044666Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-likeFamily
IA [auth t]IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
IA [auth t]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
IA [auth t]IPR026951Peptidyl-prolyl cis-trans isomerase like 2, U-box domainDomain
JA [auth m],
VA [auth f]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
JA [auth m],
VA [auth f]
IPR017131Small ribonucleoprotein associated, SmB/SmNFamily
JA [auth m],
VA [auth f]
IPR047575Sm domainDomain
JA [auth m],
VA [auth f]
IPR010920LSM domain superfamilyHomologous Superfamily
BB [auth e],
LA [auth l]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
BB [auth e],
LA [auth l]
IPR034099Small nuclear ribonucleoprotein Sm D3Family
BB [auth e],
LA [auth l]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
BB [auth e],
LA [auth l]
IPR047575Sm domainDomain
BB [auth e],
LA [auth l]
IPR010920LSM domain superfamilyHomologous Superfamily
MA [auth A]IPR012984PROCT domainDomain
MA [auth A]IPR012591PRO8NT domainDomain
MA [auth A]IPR019580Pre-mRNA-processing-splicing factor 8, U6-snRNA-bindingDomain
MA [auth A]IPR027652Pre-mRNA-processing-splicing factor 8Family
MA [auth A]IPR043172Prp8 RNase domain IV, palm regionHomologous Superfamily
MA [auth A]IPR012592PROCN domainDomain
MA [auth A]IPR012337Ribonuclease H-like superfamilyHomologous Superfamily
MA [auth A]IPR043173Prp8 RNase domain IV, fingers regionHomologous Superfamily
MA [auth A]IPR021983PRP8 domain IV coreDomain
MA [auth A]IPR019581Pre-mRNA-processing-splicing factor 8, U5-snRNA-bindingDomain
MA [auth A]IPR037518MPN domainDomain
MA [auth A]IPR019582RNA recognition motif, spliceosomal PrP8Domain
MA [auth A]IPR042516Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamilyHomologous Superfamily
MA [auth A]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
OA [auth 8]IPR019775WD40 repeat, conserved siteConserved Site
OA [auth 8]IPR032847Pre-mRNA-processing factor 17Family
OA [auth 8]IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
OA [auth 8]IPR001680WD40 repeatRepeat
OA [auth 8]IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
DB [auth c],
PA [auth j]
IPR027078Small nuclear ribonucleoprotein EFamily
DB [auth c],
PA [auth j]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
DB [auth c],
PA [auth j]
IPR047575Sm domainDomain
DB [auth c],
PA [auth j]
IPR010920LSM domain superfamilyHomologous Superfamily
RA [auth n],
XA [auth g]
IPR027141Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3Family
RA [auth n],
XA [auth g]
IPR034102Small nuclear ribonucleoprotein D1Domain
RA [auth n],
XA [auth g]
IPR001163Sm domain, eukaryotic/archaea-typeDomain
RA [auth n],
XA [auth g]
IPR047575Sm domainDomain
RA [auth n],
XA [auth g]
IPR010920LSM domain superfamilyHomologous Superfamily
SA [auth P]IPR036855Zinc finger, CCCH-type superfamilyHomologous Superfamily
SA [auth P]IPR039171Pre-mRNA-splicing factor Cwc2/Slt11Family
SA [auth P]IPR000504RNA recognition motif domainDomain
SA [auth P]IPR000571Zinc finger, CCCH-typeDomain
SA [auth P]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
SA [auth P]IPR048995STL11/RBM22-like, N-terminal domainDomain
SA [auth P]IPR035979RNA-binding domain superfamilyHomologous Superfamily
UA [auth p]IPR045146Splicing factor 3A subunit 1Family
UA [auth p]IPR035967SWAP/Surp superfamilyHomologous Superfamily
UA [auth p]IPR000061SWAP/SurpDomain
UA [auth p]IPR000626Ubiquitin-like domainDomain
UA [auth p]IPR035563Splicing factor 3A subunit 1, ubiquitin domainDomain
UA [auth p]IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
UA [auth p]IPR022030Splicing factor 3A subunit 1, conserved domainDomain
WA [auth F]IPR031781SF3A2 domainDomain
WA [auth F]IPR003604Matrin/U1-C-like, C2H2-type zinc fingerDomain
WA [auth F]IPR013087Zinc finger C2H2-typeDomain
WA [auth F]IPR036236Zinc finger C2H2 superfamilyHomologous Superfamily
WA [auth F]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
YA [auth 4]IPR021966Splicing factor SF3a60 binding domainDomain
YA [auth 4]IPR031774SF3A3 domainDomain
YA [auth 4]IPR024598Splicing factor SF3a60 /Prp9 subunit, C-terminalDomain
YA [auth 4]IPR000690Matrin/U1-C, C2H2-type zinc fingerDomain
YA [auth 4]IPR025086SDE2-like, C-terminal domainDomain
AB [auth u]IPR016024Armadillo-type foldHomologous Superfamily
AB [auth u]IPR011989Armadillo-like helicalHomologous Superfamily
AB [auth u]IPR015016Splicing factor 3B subunit 1Domain
AB [auth u]IPR038737Splicing factor 3B subunit 1-likeFamily
GA [auth o]IPR029000Cyclophilin-like domain superfamilyHomologous Superfamily
GA [auth o]IPR002130Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainDomain
GA [auth o]IPR034168Peptidyl-prolyl cis-trans isomerase E, RNA recognition motifDomain
GA [auth o]IPR016304Peptidyl-prolyl cis-trans isomerase EFamily
GA [auth o]IPR020892Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved siteConserved Site
GA [auth o]IPR000504RNA recognition motif domainDomain
GA [auth o]IPR012677Nucleotide-binding alpha-beta plait domain superfamilyHomologous Superfamily
GA [auth o]IPR035979RNA-binding domain superfamilyHomologous Superfamily
QA [auth I]IPR024767Pre-mRNA-splicing factor 38, C-terminalDomain
QA [auth I]IPR005037Pre-mRNA-splicing factor 38Family
CB [auth T]IPR006568PSP, proline-richDomain
CB [auth T]IPR007180Domain of unknown function DUF382Domain
CB [auth T]IPR003034SAP domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A [auth D]PharosQ96DI7
B [auth E]PharosQ15393
C [auth b],
HA [auth i]
PharosP62306
E [auth w]PharosQ15427
F [auth d],
NA [auth k]
PharosP62308
G [auth U]PharosO60306
H [auth x]PharosQ9BWJ5
J [auth B]PharosP08579
K [auth z]PharosQ9Y3B4
L [auth q]PharosQ9BZL1
M [auth s]PharosO75643
N [auth v]PharosQ13573
O [auth 3]PharosQ9BRD0
P [auth 0]PharosQ8TAD8
PharosP41223
S [auth L]PharosQ99459
T [auth N]PharosQ96NC0
U [auth S]PharosQ8WYA6
V [auth r]PharosQ15029
W [auth R]PharosQ9P013
X [auth Y]PharosQ8IYB3
Y [auth 7]PharosO60870
Z [auth M]PharosQ9HCS7
AA [auth K]PharosP55081
BA [auth O]PharosQ9BZJ0
CA [auth y]PharosQ7RTV0
EA [auth G]PharosO43660
FA [auth h],
ZA [auth a]
PharosP62316
IA [auth t]PharosQ13356
JA [auth m],
VA [auth f]
PharosP14678
BB [auth e],
LA [auth l]
PharosP62318
MA [auth A]PharosQ6P2Q9
OA [auth 8]PharosO60508
DB [auth c],
PA [auth j]
PharosP62304
RA [auth n],
XA [auth g]
PharosP62314
SA [auth P]PharosQ9NW64
UA [auth p]PharosQ15459
WA [auth F]PharosQ15428
YA [auth 4]PharosQ12874
AB [auth u]PharosO75533
GA [auth o]PharosQ9UNP9
QA [auth I]PharosQ8NAV1
CB [auth T]PharosQ13435