Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148940 228 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 303
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148940 228 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 303
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940   180 IKCEVAVSSIISASHFFIQQptHPSFASLRHLDMYMGSLYGEQSNlPELPIPCQNGLLCAAPVGNAWFRAVtVQYFDETD 259
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKWYRAK-ITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 25148940   260 EVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAH 300
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117

K homology RNA-binding domain;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25148940     74 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKThqicqVRGKRDEINHCLQMLRRR 140
Cdd:smart00322   6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVE-----ITGPPENVEKAAELILEI 67

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148940 228 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 303
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940   180 IKCEVAVSSIISASHFFIQQptHPSFASLRHLDMYMGSLYGEQSNlPELPIPCQNGLLCAAPVGNAWFRAVtVQYFDETD 259
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKWYRAK-ITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 25148940   260 EVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAH 300
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25148940  74 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDkvkTHQICQVRGKRDEINHCLQMLR 138
Cdd:cd00105   2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGS---GERVVTITGTPEAVEKAKELIE 63

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 215 MGSLYGEQSNLPELPIPcQNGLLCAAPV--GNAWFRAVTVQyFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQ 292
Cdd:cd20412  13 MTQYYESEENRHTLLTV-QVGDIVAAPFrhDGSWYRARVLG-FLENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQ 90

                ...
gi 25148940 293 STE 295
Cdd:cd20412  91 AIE 93

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 184 VAVSSIISASHFFIQQPTHPSFASLRHLDMYMGSLYgEQSNLPELPIPCQnGLLCAA--PVGNAWFRAV--TVQYFDETD 259
Cdd:cd20408   1 GTVTEFKNPGEFYIQIYTLEVLESLVKLTSQLKKTY-ASVNNHKEYIPEV-GEVCVAkySEDQNWYRALvqTVDVQQKKA 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25148940 260 EVFvkFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGttNWSDAAM 315
Cdd:cd20408  79 GVF--YIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSG--SWSEECI 130

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 25148940    235 GLLCAAPVGN-AWFRAVTVQYfDETDEVFVKFVDYGGYSKMARQDLRQIRTDL 286
Cdd:smart00333   6 GDKVAARWEDgEWYRARIVKV-DGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25148940  72 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRmlIRQHHETDKVKTHQIcQVRGKRDEINHCLQMLRRR 140
Cdd:cd22454   5 TIEVVIPNADVGKVIGKGGETIKRIEALTDTV--ITFERVNGGSPNREV-QITGSPDNVAAAKRLIEDT 70

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25148940 246 WFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDG 306
Cdd:cd20423  19 WCRALIDNVYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPSG 79

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 182 CEVAVSSIISASHFFIQQPThpsfASLRHLDMYMGSLyGEQSNLPELPIPC---QNGLLCAAPVGNAWFRAVTVQYFDet 258
Cdd:cd20426   1 IEAYATAVDSPEYFWCQFAT----EKIQCLAVKVQEA-GEQVADRGNFIPSiyvGDPCIVKYSEDNHWYRALVTKIND-- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 259 DEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKF 318
Cdd:cd20426  74 NLVSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSEGL--WSDEANDYF 131

seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25148940 221 EQSNLPELPIpcQNGLLCAAPV--GNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQS 293
Cdd:cd20442  41 KCKFVPVEDI--KEGLECLAKSkkNLKWYRAVVEHLYPETEKMLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQA 113

sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 181 KCEVAVSSIISASHFFIQQPTHPSFASLRHLDMYMGSLYGEQSNLPELpipcQNG-LLCAA-PVGNAWFRAV-TVQYFDe 257
Cdd:cd20425   1 KTEVYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDEEVECESL----QLGdLICAEyPEDGLWYRAVvKEKIPN- 75

                        90       100       110
                ....*....|....*....|....*....|...
gi 25148940 258 tDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLP 290
Cdd:cd20425  76 -NLVSVQFIDYGNTSVVQPSKIHRLPKELLSIP 107

second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the second one.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 25148940  74 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 108
Cdd:cd22397   3 EIMIPGNKVGLIIGKGGETIKQLQERAGVKMVMIQ 37

second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 183 EVAVSSIISASHFFIQQPThpSFASLRHLDMYMGSLYGEQSNlpELPIPCQN-GLLCAAPVGNA-WFRAVtVQYFDETDE 260
Cdd:cd20437   6 KVKITAAVSPSKFYCQLLS--WEPELSKLTTQMTLHYESVSK--ELNPSCENfGLLCAAKGKDGqWHRGF-LQQLLPPSQ 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 25148940 261 VFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQS 293
Cdd:cd20437  81 VKVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMS 113

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 182 CEVAVSSIISASHFFIQQPTHPSfaSLRHLDMYMGSLYGEQSNLPELPIPCQNGLLCAAPVG-NAWFRAVTVQYFDETDE 260
Cdd:cd20422   2 YDAQVEFVKDPSEFWIRLGEHAV--PFSKLMRSMTAFYSQASKLDGVVLKPQPGQLCCAKWKeDRYYRAIVTAVKGKMVE 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25148940 261 VFvkFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKFR 319
Cdd:cd20422  80 VF--LVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICPLGER--WSPEAISAFK 134

fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25148940  73 YEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKthQICQVRGKRDEINHCLQMLRRR 140
Cdd:cd22399   2 VTFLVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPPNPNE--KLFIIRGNPQQIEHAKQLIREK 67

third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25148940  72 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMlirQHHETDKVKTHQICQVRGKRDEINHCLQMLR 138
Cdd:cd22398   1 GMEVPVPRFAVGVVIGKGGEMIKKIQNETGARV---QFKPDDGNSPDRICVITGPPDQVQHAARMIQ 64

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148940 186 VSSIISASHFFIQQPTHPS-FASLRH--LDMYmgSLYGEQSNLPELPIPcqnGLLCAAPVGN--AWFRAVTVQYFDetDE 260
Cdd:cd20438  11 VEYVLNPSNFWIRTDEYNNeFQALMKniADIY--NLCGNDEELLKKPEP---GLLCCARYSKdrHYYRAVITEVLD--LK 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25148940 261 VFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKFR 319
Cdd:cd20438  84 VSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEV--WTKNANDFFK 140

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.

                        10        20        30
                ....*....|....*....|....*....|..
gi 25148940  75 FEIPNSLVGLIIGVKGKTIKELSVRTNVRMLI 106
Cdd:cd22446  11 ISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQI 42

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 25148940  72 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 108
Cdd:cd22481   3 VQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQ 39

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 25148940  72 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 108
Cdd:cd22482   3 VQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQ 39

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 25148940  72 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 108
Cdd:cd02393   5 ITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED 41

first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25148940  77 IPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKTHQICQVRGKRDEINHCLQML 137
Cdd:cd22435   8 VPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDFYPGTTERVCLIQGEVEAVNAVLDFI 68

type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex subunit 1 (ASCC1) and similar proteins; ASCC1, also called ASC-1 complex subunit p50, or Trip4 complex subunit p50, plays a role in DNA damage repair as component of the ASCC complex. It is part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. ASCC1 may also play a role in the development of neuromuscular junction.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 25148940  73 YEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLI-RQHHETD 113
Cdd:cd22419   3 LSLDVPSALFKFIIGKKGETKKRLESETKTQIRIpRQGKEGD 44