OCRE domain found in RNA-binding protein RBM5, RBM10, and similar proteins; RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing, and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17508949 554 PPNPLTFAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWDLTHHTYFPVET 608
Cdd:cd16162   2 PPDPSTYQYDETSGYYYDPTTGLYYDPNSQYFYNSQTQQYLYWDQTKKTYVPVPT 56

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 222 PSNKLAILNMPNDVDNTKITLSLGKCGYLP-QDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGWLTLD--DGR 298
Cdd:cd12313   1 PTNVLILRGLDVLTTEEDILSALQAHADLPiKDVRLIR--DKLTGTSRGFAFVEFSSLEDATQVMDALQNLLPPFkiDGR 78

                ....*..
gi 17508949 299 TLAVEYA 305
Cdd:cd12313  79 VVSVSYA 85

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 361 PCDTLLIRGLPDGINNSLIFDSLGALVCLSsISMIKL------SESKRFAYLQMKSADEAKMLLNLTYKS--PIRIKDKD 432
Cdd:cd12313   1 PTNVLILRGLDVLTTEEDILSALQAHADLP-IKDVRLirdkltGTSRGFAFVEFSSLEDATQVMDALQNLlpPFKIDGRV 79

                ....*.
gi 17508949 433 VQVSWC 438
Cdd:cd12313  80 VSVSYA 85

OCRE domain found in RNA-binding protein RBM5, RBM10, and similar proteins; RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing, and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17508949 554 PPNPLTFAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWDLTHHTYFPVET 608
Cdd:cd16162   2 PPDPSTYQYDETSGYYYDPTTGLYYDPNSQYFYNSQTQQYLYWDQTKKTYVPVPT 56

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 17508949   855 SNIGNRLLKSMGWKEGQGVGKHAQGIVNPIEAERFVQGAGLGA 897
Cdd:pfam01585   2 SNIGFKLLQKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGLGA 44

RNA recognition motif 1 (RRM1) and 2 (RRM2) found in RNA-binding protein 5 (RBM5) and similar proteins; This subfamily includes the RRM1 and RRM2 of RNA-binding protein 5 (RBM5 or LUCA15 or H37) and RNA-binding protein 10 (RBM10 or S1-1), and the RRM2 of RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). These RBMs share high sequence homology and may play an important role in regulating apoptosis. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM6 has been predicted to be a nuclear factor based on its nuclear localization signal. Both, RBM6 and RBM5, specifically bind poly(G) RNA. RBM10 is a paralog of RBM5. It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. All family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 222 PSNKLAILNMPNDVDNTKITLSLGKCGYLP-QDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGWLTLD--DGR 298
Cdd:cd12313   1 PTNVLILRGLDVLTTEEDILSALQAHADLPiKDVRLIR--DKLTGTSRGFAFVEFSSLEDATQVMDALQNLLPPFkiDGR 78

                ....*..
gi 17508949 299 TLAVEYA 305
Cdd:cd12313  79 VVSVSYA 85

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508949    230 NMPNDVDNTKITLSLGKCGYLpQDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGwLTLdDGRTLAV 302
Cdd:smart00360   6 NLPPDTTEEELRELFSKFGKV-ESVRLVR--DKETGKSKGFAFVEFESEEDAEKALEALNG-KEL-DGRPLKV 73

Zn-finger in Ran binding protein and others;

                          10        20
                  ....*....|....*....|....*.
gi 17508949   318 DDWICAHCSMNNFVKRQTCFKCEISK 343
Cdd:pfam00641   3 GDWDCSKCLVQNFATSTKCVACQAPK 28

RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17508949 252 QDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGwlTLDDGRTLAVEYAK 306
Cdd:COG0724  29 TSVKLIT--DRETGRSRGFGFVEMPDDEEAQAAIEALNG--AELMGRTLKVNEAR 79

OCRE domain found in RNA-binding protein RBM5, RBM10, and similar proteins; RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor; it specifically binds poly(G) RNA. RBM10, a paralog of RBM5, may play an important role in mRNA generation, processing, and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. Both RBM5 and RBM10, contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17508949 554 PPNPLTFAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWDLTHHTYFPVET 608
Cdd:cd16162   2 PPDPSTYQYDETSGYYYDPTTGLYYDPNSQYFYNSQTQQYLYWDQTKKTYVPVPT 56

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 17508949   855 SNIGNRLLKSMGWKEGQGVGKHAQGIVNPIEAERFVQGAGLGA 897
Cdd:pfam01585   2 SNIGFKLLQKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGLGA 44

OCRE domain found in RNA-binding protein 5 (RBM5) and similar proteins; RBM5 is also called protein G15, H37, putative tumor suppressor LUCA15, or renal carcinoma antigen NY-REN-9. It is a known modulator of apoptosis. It acts as a tumor suppressor or an RNA splicing factor. RBM5 shows high sequence similarity to RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). Both of them specifically binds poly(G) RNA. RBM5 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508949 555 PNPLTFAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWDLTHHTYFP 605
Cdd:cd16168   3 PDTSTYQYDESSGYYYDPITGLYYDPNSQYYYNSLTQQYLYWDGEKQTYLP 53

OCRE domain; The OCRE (OCtamer REpeat) domain contains 5 repeats of an 8-residue motif, which were shown to form beta-strands. Based on the architectures of proteins containing OCRE domains, a role in RNA metabolism and/or signalling has been proposed.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508949 554 PPNPLTFAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWDLTHHTYFPV 606
Cdd:cd16074   2 SPDPSGFVFDPNSGYYYDPSTGLYYDPNTGYYYDPTSGTYYIWDDELGAYVPV 54

RNA recognition motif 1 (RRM1) and 2 (RRM2) found in RNA-binding protein 5 (RBM5) and similar proteins; This subfamily includes the RRM1 and RRM2 of RNA-binding protein 5 (RBM5 or LUCA15 or H37) and RNA-binding protein 10 (RBM10 or S1-1), and the RRM2 of RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). These RBMs share high sequence homology and may play an important role in regulating apoptosis. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM6 has been predicted to be a nuclear factor based on its nuclear localization signal. Both, RBM6 and RBM5, specifically bind poly(G) RNA. RBM10 is a paralog of RBM5. It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. All family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 222 PSNKLAILNMPNDVDNTKITLSLGKCGYLP-QDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGWLTLD--DGR 298
Cdd:cd12313   1 PTNVLILRGLDVLTTEEDILSALQAHADLPiKDVRLIR--DKLTGTSRGFAFVEFSSLEDATQVMDALQNLLPPFkiDGR 78

                ....*..
gi 17508949 299 TLAVEYA 305
Cdd:cd12313  79 VVSVSYA 85

OCRE domain found in RNA-binding protein 6 (RBM6) and similar proteins; RBM6, also called lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3, has been predicted to be a nuclear factor based on its nuclear localization signal. It shows high sequence similarity to RNA-binding protein 5 (RBM5 or LUCA15 or NY-REN-9). Both specifically binds poly(G) RNA. RBM6 contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has an additional unique domain, the POZ (poxvirus and zinc finger) domain, which may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17508949 545 PKGLLPRY-LPPNPlTFAHDPNLGYYVDPITKFCYDSATGYY 585
Cdd:cd16163   2 GSGPAPTYrSDPDS-GYIYDPETGYYYDPVTGLYYDPATGEY 42

RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 10 (RBM10); This subgroup corresponds to the RRM1 of RBM10, also termed G patch domain-containing protein 9, or RNA-binding protein S1-1 (S1-1), a paralog of putative tumor suppressor RNA-binding protein 5 (RBM5 or LUCA15 or H37). It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. RBM10 is structurally related to RBM5 and RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). It contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 223 SNKLAILNMPNDVDNTKITLSLGKCGYLPQDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGWLTLdDGRTLAV 302
Cdd:cd12753   1 SNIIMLRMLPQSATENDIRGQLQAHGVQPREVRLMR--NKSSGQSRGFAFVEFNHLQDATRWMEANQHSLTI-LGQKVSM 77

                ....*..
gi 17508949 303 EYAKGDP 309
Cdd:cd12753  78 HYSDPKP 84

RNA recognition motif;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508949    230 NMPNDVDNTKITLSLGKCGYLpQDVRTMTkfDKNTKQIRTFAFVEFSNRETAEQWMTDYEGwLTLdDGRTLAV 302
Cdd:smart00360   6 NLPPDTTEEELRELFSKFGKV-ESVRLVR--DKETGKSKGFAFVEFESEEDAEKALEALNG-KEL-DGRPLKV 73

RNA recognition motif 1 (RRM1) and 2 (RRM2) found in RNA-binding protein 5 (RBM5) and similar proteins; This subfamily includes the RRM1 and RRM2 of RNA-binding protein 5 (RBM5 or LUCA15 or H37) and RNA-binding protein 10 (RBM10 or S1-1), and the RRM2 of RNA-binding protein 6 (RBM6 or NY-LU-12 or g16 or DEF-3). These RBMs share high sequence homology and may play an important role in regulating apoptosis. RBM5 is a known modulator of apoptosis. It may also act as a tumor suppressor or an RNA splicing factor. RBM6 has been predicted to be a nuclear factor based on its nuclear localization signal. Both, RBM6 and RBM5, specifically bind poly(G) RNA. RBM10 is a paralog of RBM5. It may play an important role in mRNA generation, processing and degradation in several cell types. The rat homolog of human RBM10 is protein S1-1, a hypothetical RNA binding protein with poly(G) and poly(U) binding capabilities. All family members contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, and a G-patch/D111 domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 361 PCDTLLIRGLPDGINNSLIFDSLGALVCLSsISMIKL------SESKRFAYLQMKSADEAKMLLNLTYKS--PIRIKDKD 432
Cdd:cd12313   1 PTNVLILRGLDVLTTEEDILSALQAHADLP-IKDVRLirdkltGTSRGFAFVEFSSLEDATQVMDALQNLlpPFKIDGRV 79

                ....*.
gi 17508949 433 VQVSWC 438
Cdd:cd12313  80 VSVSYA 85

RNA recognition motif (RRM) found in Helicobacter pylori HP0827 protein and similar proteins; This subfamily corresponds to the RRM of H. pylori HP0827, a putative ssDNA-binding protein 12rnp2 precursor, containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The ssDNA binding may be important in activation of HP0827.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 226 LAILNMPNDVDNTKITLSLGKCGYLpQDVRTMtkFDKNTKQIRTFAFVEFSNRETAEQWMTDYEGwlTLDDGRTLAVEYA 305
Cdd:cd12399   1 LYVGNLPYSASEEQLKSLFGQFGAV-FDVKLP--MDRETKRPRGFGFVELQEEESAEKAIAKLDG--TDFMGRTIRVNEA 75

RED-like protein N-terminal region; This family contains sequences that are similar to the N-terminal region of Red protein. This and related proteins contain a RED repeat which consists of a number of RE and RD sequence elements. The region in question has several conserved NLS sequences and a putative trimeric coiled-coil region, suggesting that these proteins are expressed in the nucleus. The function of Red protein is unknown, but efficient sequestration to nuclear bodies suggests that its expression may be tightly regulated of that the protein self-aggregates extremely efficiently.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508949   785 LQEEEEDASAPDLPKivYRDRAKERRRQFGID-------STGYAFDVMgGPPGPTSVRHEETiRKVSEEASK 849
Cdd:pfam07808   1 LKKQEEDKLAELAPK--YRDRAKERREGANPDyqnedpvSTTSAYRAV-APDAKSGLDAAER-RKQMIQESK 68

RNA recognition motif 1 (RRM1) found in fission yeast pre-mRNA-splicing factor Srp1p and similar proteins; This subgroup corresponds to the RRM domain in Srp1p encoded by gene srp1 from fission yeast Schizosaccharomyces pombe. It plays a role in the pre-mRNA splicing process, but not essential for growth. Srp1p is closely related to the SR protein family found in metazoa. It contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a glycine hinge and a RS domain in the middle, and a C-terminal domain. Some family members also contain another RRM domain.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17508949 264 TKQIRTFAFVEFSNRETAEQWMTDYEGWLTLDDGRTLAVEYAK 306
Cdd:cd12467  36 TFQSRPFAFVEYESHRDAEDAYEEMHGRRFPDTGDTLHVQWAK 78

RNA recognition motif (RRM) found in Saccharomyces cerevisiae nucleolar protein 6 (Nop6) and similar proteins; This subfamily corresponds to the RRM of Nop6, also known as Ydl213c, a component of 90S pre-ribosomal particles in yeast S. cerevisiae. It is enriched in the nucleolus and is required for 40S ribosomal subunit biogenesis. Nop6 is a non-essential putative RNA-binding protein with two N-terminal putative nuclear localisation sequences (NLS-1 and NLS-2) and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). It binds to the pre-rRNA early during transcription and plays an essential role in pre-rRNA processing.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17508949 230 NMPNDVDNTKITLSLGKCGYlPQDVRTMTkfDKNTKQIRTFAFVEFSNRE 279
Cdd:cd12400   7 NLPYDTTAEDLKEHFKKAGE-PPSVRLLT--DKKTGKSKGCAFVEFDNQK 53

OCRE domain found in angiogenic factor VG5Q and similar proteins; VG5Q, also called angiogenic factor with G patch and FHA domains 1 (AGGF1), or G patch domain-containing protein 7, or vasculogenesis gene on 5q protein, functions as a potent angiogenic factor in promoting angiogenesis through interacting with TWEAK (also known as TNFSF12), which is a member of the tumor necrosis factor (TNF) superfamily that induces angiogenesis in vivo. VG5Q can bind to the surface of endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. The chromosomal translocation t(5;11) and the E133K variant in VG5Q are associated with Klippel-Trenaunay syndrome (KTS), a disorder characterized by diverse effects in the vascular system. In addition to a forkhead-associated (FHA) domain and a G-patch motif, VG5Q contains an N-terminal OCtamer REpeat (OCRE) domain that is characterized by a 5-fold, imperfectly repeated octameric sequence.

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17508949 560 FAHDPNLGYYVDPITKFCYDSATGYYFNNATSQWCNWD 597
Cdd:cd16164   8 FVYDEATGMYYDPSTGYYYDSETQLYYDPNTGTYYYYD 45

RNA recognition motif 1 (RRM1) found in tRNA selenocysteine-associated protein 1 (SECp43) and similar proteins; This subfamily corresponds to the RRM1 in tRNA selenocysteine-associated protein 1 (SECp43), yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8, and similar proteins. SECp43 is an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region. Yeast proteins, NGR1 and NAM8, show high sequence similarity with SECp43. NGR1 is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA). It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains three RRMs, two of which are followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the C-terminus which also harbors a methionine-rich region. NAM8 is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. NAM8 also contains three RRMs.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508949 231 MPNDVDNTKITLSLGKCGYLPQDVRTMtkFDKNTKQIRTFAFVEFSNRETAEQWMTDYEG 290
Cdd:cd12344   7 LEPWMDEAYISSCFAKTGEEVVSVKII--RNKQTGKSAGYCFVEFATQEAAEQALEHLNG 64

RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 subunit G (eIF-3G) and similar proteins; This subfamily corresponds to the RRM of eIF-3G and similar proteins. eIF-3G, also termed eIF-3 subunit 4, or eIF-3-delta, or eIF3-p42, or eIF3-p44, is the RNA-binding subunit of eIF3, a large multisubunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3G binds 18 S rRNA and beta-globin mRNA, and therefore appears to be a nonspecific RNA-binding protein. eIF-3G is one of the cytosolic targets and interacts with mature apoptosis-inducing factor (AIF). eIF-3G contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). This family also includes yeast eIF3-p33, a homolog of vertebrate eIF-3G, plays an important role in the initiation phase of protein synthesis in yeast. It binds both, mRNA and rRNA, fragments due to an RRM near its C-terminus.

                        10        20
                ....*....|....*....|...
gi 17508949 261 DKNTKQIRTFAFVEFSNRETAEQ 283
Cdd:cd12408  34 DKETGQSKGFAFVTFETREDAER 56