Drosophila_melanogasterFamily: RRM_1 Number of Genes: 129
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
bru1
Hrb98DE
mod
sm
snf
tra2
nonA
Hrb87F
B52
Hrb27C
orb
Rb97D
U2af50
Pabp2
Rox8
Rbp4
Rbp9
Ref1
bol
heph
Rsf1
lark
msi
Rnp4F
nonA-l
rin
Spx
spen
snRNP-U1-70K
Nelf-E
U2af38
eIF4B
Cbp20
Srp54
Neos
ssx
TBPH
fz3
nito
CG5808
CstF64
cyp33
CG4119
x16
hfp
eIF3g1
CG6999
Rbp1-like
CG10993
CG14414
CG18259
CG6961
CG14230
CG11454
CG4887
CG4896
CG15440
CG3294
Caper
Ref2
CG12288
CG10466
tsu
eIF3b
CG9346
CG4266
LS2
CG4612
Pof
CG3594
CG7879
CG1316
Sf3b6
CG7185
CG3335
CG11726
CG10948
CG7804
barc
CG14641
srl
CG2931
SLIRP2
RnpS1
CG14718
CG5213
eIF3g2
Syp
CG6937
Saf-B
CG14506
CG7903
eIF4H2
Set1
CG14628
CG18823
Cnot4
Rbfox1
shep
CG32706
SLIRP1
CG34354
trv
CG40813
CG41562
fne
Spf45
glo
CG42458
elav
CG4806
Larp7
Rbp6
Rbp1
bru2
eIF4H1
sqd
CG34334
cpo
bru3
Sxl
orb2
CG44249
pAbp
SC35
rump
SF2
Imp
caz

Introduction

Pfam

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. 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 (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 (P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

InterPro

Many eukaryotic proteins containing one or more copies of a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs [PUBMED:3072706, PUBMED:3192525, PUBMED:3313012]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence [PUBMED:2470643, PUBMED:2467746]. RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu) [PUBMED:3192525, PUBMED:3313012, PUBMED:2467746]. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialised features for protein recognition [PUBMED:15231733]. The motif also appears in a few single stranded DNA binding proteins.

Reference

  1. Birney E., Kumar S., Krainer A.R. , Nucleic Acid Res 1993;21:5803-5816.: Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. PUBMED:8290338 EPMC:8290338.