RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins; This model corresponds to the RRM of NOL8 (also termed Nop132) encoded by a novel NOL8 gene that is up-regulated in the majority of diffuse-type, but not intestinal-type, gastric cancers. Thus, NOL8 may be a good molecular target for treatment of diffuse-type gastric cancer. Also, NOL8 is a phosphorylated protein that contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), suggesting NOL8 is likely to function as a novel RNA-binding protein. It may be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGEYvgsGQDVFERH-----NGFAFVTMRFEDAeALQRLKSRFHKVKFKGNQLIVD 79
Cdd:cd12226    1 RLFVGGLSPSITE--DDLERRFSRFGTV---SDVEIIRKkdapdRGFAYIDLRTSEA-ALQKCLSTLNGVKWKGSRLKIQ 74

                 ...
gi 961785146  80 YAR 82
Cdd:cd12226   75 LAK 77

RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins; This model corresponds to the RRM of NOL8 (also termed Nop132) encoded by a novel NOL8 gene that is up-regulated in the majority of diffuse-type, but not intestinal-type, gastric cancers. Thus, NOL8 may be a good molecular target for treatment of diffuse-type gastric cancer. Also, NOL8 is a phosphorylated protein that contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), suggesting NOL8 is likely to function as a novel RNA-binding protein. It may be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGEYvgsGQDVFERH-----NGFAFVTMRFEDAeALQRLKSRFHKVKFKGNQLIVD 79
Cdd:cd12226    1 RLFVGGLSPSITE--DDLERRFSRFGTV---SDVEIIRKkdapdRGFAYIDLRTSEA-ALQKCLSTLNGVKWKGSRLKIQ 74

                 ...
gi 961785146  80 YAR 82
Cdd:cd12226   75 LAK 77

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961785146     5 RLFIGNLKHGVEEclADLEQRFKAFGEYVGS---GQDVFERHNGFAFVTmrFEDAEALQRLKSRFHKVKFKGNQLIV 78
Cdd:smart00360   1 TLFVGNLPPDTTE--EELRELFSKFGKVESVrlvRDKETGKSKGFAFVE--FESEEDAEKALEALNGKELDGRPLKV 73

RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins; This model corresponds to the RRM of NOL8 (also termed Nop132) encoded by a novel NOL8 gene that is up-regulated in the majority of diffuse-type, but not intestinal-type, gastric cancers. Thus, NOL8 may be a good molecular target for treatment of diffuse-type gastric cancer. Also, NOL8 is a phosphorylated protein that contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), suggesting NOL8 is likely to function as a novel RNA-binding protein. It may be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGEYvgsGQDVFERH-----NGFAFVTMRFEDAeALQRLKSRFHKVKFKGNQLIVD 79
Cdd:cd12226    1 RLFVGGLSPSITE--DDLERRFSRFGTV---SDVEIIRKkdapdRGFAYIDLRTSEA-ALQKCLSTLNGVKWKGSRLKIQ 74

                 ...
gi 961785146  80 YAR 82
Cdd:cd12226   75 LAK 77

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961785146     5 RLFIGNLKHGVEEclADLEQRFKAFGEYVGS---GQDVFERHNGFAFVTmrFEDAEALQRLKSRFHKVKFKGNQLIV 78
Cdd:smart00360   1 TLFVGNLPPDTTE--EELRELFSKFGKVESVrlvRDKETGKSKGFAFVE--FESEEDAEKALEALNGKELDGRPLKV 73

RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ribonucleoprotein (NsCP33) and similar proteins; The family includes NsCP33, Arabidopsis thaliana chloroplastic 31 kDa ribonucleoprotein (CP31A) and mitochondrial glycine-rich RNA-binding protein 2 (AtGR-RBP2). NsCP33 may be involved in splicing and/or processing of chloroplast RNA's. AtCP31A, also called RNA-binding protein 1/2/3 (AtRBP33), or RNA-binding protein CP31A, or RNA-binding protein RNP-T, or RNA-binding protein cp31, is required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs, as well as for normal chloroplast development under cold stress conditions by stabilizing transcripts of numerous mRNAs under these conditions. CP31A may modulate telomere replication through RNA binding domains. AtGR-RBP2, also called AtRBG2, or glycine-rich protein 2 (AtGRP2), or mitochondrial RNA-binding protein 1a (At-mRBP1a), plays a role in RNA transcription or processing during stress. It binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. AtGR-RBP2 displays strong affinity to poly(U) sequence. It exerts cold and freezing tolerance, probably by exhibiting an RNA chaperone activity during the cold and freezing adaptation process. Some members in this family contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The model corresponds to the second RRM motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGEyVGSGQDVFERHNG----FAFVTmrFEDAEALQRLKSRFHKVKFKGNQLIVDY 80
Cdd:cd21608    1 KLYVGNLSWDTTE--DDLRDLFSEFGE-VESAKVITDRETGrsrgFGFVT--FSTAEAAEAAIDALNGKELDGRSIVVNE 75

                 .
gi 961785146  81 A 81
Cdd:cd21608   76 A 76

RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 18 and similar proteins; This subfamily corresponds to the RRM of RBM18, a putative RNA-binding protein containing a well-conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of RBM18 remains unclear.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGE-------YVGSGQDVFERHnGFAFVTmrFEDAEALQRLKSRFHKVKFKGNQLI 77
Cdd:cd12355    1 RLWIGNLDPRLTE--YHLLKLLSKYGKikkfdflFHKTGPLKGQPR-GYCFVT--FETKEEAEKAIECLNGKLALGKKLV 75

                 ....*
gi 961785146  78 VDYAR 82
Cdd:cd12355   76 VRWAH 80

RNA recognition motif 1 (RRM1) found in Schizosaccharomyces pombe meiotically up-regulated gene 28 protein (Mug28) and similar proteins; Mug28 is a meiosis-specific protein that regulates spore wall formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The model corresponds to the first RRM motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   3 EKRLFIGNLKHGVEEclADLEQRFKAFGEYVGSgqDVFER-HNG---------FAFVTmrFEDAEALQRLKSRFHKVKFK 72
Cdd:cd21620    1 ERSLYVGNLPQTCQS--EDLIILFEPYGNVCGA--HIASRkKVKvswvkpsklFAFVE--FETKEAATTAIVLLNGITYM 74

                         90
                 ....*....|
gi 961785146  73 GNQLIVDYAR 82
Cdd:cd21620   75 GCQLKVEWSH 84

RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 3 (SRSF3) and similar proteins; This subfamily corresponds to the RRM of two serine/arginine (SR) proteins, serine/arginine-rich splicing factor 3 (SRSF3) and serine/arginine-rich splicing factor 7 (SRSF7). SRSF3, also termed pre-mRNA-splicing factor SRp20, modulates alternative splicing by interacting with RNA cis-elements in a concentration- and cell differentiation-dependent manner. It is also involved in termination of transcription, alternative RNA polyadenylation, RNA export, and protein translation. SRSF3 is critical for cell proliferation, and tumor induction and maintenance. It can shuttle between the nucleus and cytoplasm. SRSF7, also termed splicing factor 9G8, plays a crucial role in both constitutive splicing and alternative splicing of many pre-mRNAs. Its localization and functions are tightly regulated by phosphorylation. SRSF7 is predominantly present in the nuclear and can shuttle between nucleus and cytoplasm. It cooperates with the export protein, Tap/NXF1, helps mRNA export to the cytoplasm, and enhances the expression of unspliced mRNA. Moreover, SRSF7 inhibits tau E10 inclusion through directly interacting with the proximal downstream intron of E10, a clustering region for frontotemporal dementia with Parkinsonism (FTDP) mutations. Both SRSF3 and SRSF7 contain a single N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal RS domain rich in serine-arginine dipeptides. The RRM domain is involved in RNA binding, and the RS domain has been implicated in protein shuttling and protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961785146   5 RLFIGNLKHGVEEclADLEQRFKAFGEYvgsgQDVFERHN--GFAFVTmrFEDAE----ALQRLKSRfhkvKFKGNQLIV 78
Cdd:cd12373    1 KVYVGNLGPRVTK--RELEDAFEKYGPL----RNVWVARNppGFAFVE--FEDPRdaedAVRALDGR----RICGSRVRV 68

                 ....*
gi 961785146  79 DYARP 83
Cdd:cd12373   69 ELSRG 73