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 967042226 760 LPTPVEITVICAAPgADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMP 836
Cdd:cd20407    1 LPEPIEVGVICAAP-VMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

RNase Y N-terminal region;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967042226  305 EESLDRNEENLDRNEESLDRNEEGLDRNEEGLDRNGEGLDRNEEIEQAAFQIISQVISEATEQVL 369
Cdd:pfam12072  91 EETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL 155

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 967042226 760 LPTPVEITVICAAPgADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMP 836
Cdd:cd20407    1 LPEPIEVGVICAAP-VMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967042226  713 ITVEVIVVNQVNAGHLFVQQHthPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGaDGAWWRAQVVASyEETN 792
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPK--SDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSE-DGKWYRAKITES-LDDG 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 967042226  793 EVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLL 831
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115

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 967042226   761 PTPVEITViCAAPGADGAWWRAQVVAsYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDF 819
Cdd:smart00333   1 PTFKVGDK-VAARWEDGEWYRARIVK-VDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57

RNase Y N-terminal region;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967042226  305 EESLDRNEENLDRNEESLDRNEEGLDRNEEGLDRNGEGLDRNEEIEQAAFQIISQVISEATEQVL 369
Cdd:pfam12072  91 EETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL 155

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 967042226 760 LPTPVEITVICAAPgADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMP 836
Cdd:cd20407    1 LPEPIEVGVICAAP-VMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967042226  713 ITVEVIVVNQVNAGHLFVQQHthPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGaDGAWWRAQVVASyEETN 792
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPK--SDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSE-DGKWYRAKITES-LDDG 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 967042226  793 EVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLL 831
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967042226  614 IWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLI 676
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALI 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967042226 769 ICAAPGA-DGAWWRAQVVASYEETNeVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAE 828
Cdd:cd20412   34 IVAAPFRhDGSWYRARVLGFLENGN-LDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIE 93

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 967042226   761 PTPVEITViCAAPGADGAWWRAQVVAsYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDF 819
Cdd:smart00333   1 PTFKVGDK-VAARWEDGEWYRARIVK-VDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57

type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic recombination 1 protein (MER1) and similar proteins; MER1 is required for chromosome pairing and genetic recombination. It may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967042226 613 IIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPyTQSVQICHIEGSQHHVDKALNLI 676
Cdd:cd22458    1 VTWEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPIS-NSSQQTIHLSGTDKQIALAISSI 63

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 967042226 717 VIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPvEITVICAAPGA-DGAWWRAQVVASYEETNEVE 795
Cdd:cd20408    1 GTVTEFKNPGEFYIQIYTLEVLESLVKLTSQLKKTYASVNNHKEYIP-EVGEVCVAKYSeDQNWYRALVQTVDVQQKKAG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 967042226 796 IRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDdqFSPEA 847
Cdd:cd20408   80 VFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSGS--WSEEC 129

second 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 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 967042226 712 GITVEVIVVNQVNAGHLFVQQHTHPtfHALRSLDQQMYLCY-SQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEE 790
Cdd:cd20421   10 GVTETVVVTEVTDPHRIFCQLRSLS--QELKRLSESMHQYYeGRVGSGYETRPEKLGSPCAARGSDGRWYRAVLQQVFSA 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 967042226 791 TNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLP 823
Cdd:cd20421   88 NRVVEVLHVDYGRKEVVSVSNLRYLAPEYFRMP 120

third 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 third one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYIS----TLPYTQSvQICHIEGSQHHVDKALNLIGKK 679
Cdd:cd09031    4 ELEVPENLVGAILGKGGKTLVEIQELTGARIQISkkgeFVPGTRN-RKVTITGTPAAVQAAQYLIEQR 70

second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPY-TQS-VQICHIEGSQHHVDKALNLIGKKFKE 682
Cdd:cd22429    5 ELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRESDdTLDlVRLITITGTKKEVDAAKSLILEKVSE 73

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967042226 767 TVICAAP-GADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLS 838
Cdd:cd20423    6 NPVCLAKySEDGKWCRALIDNVYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPS 78

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or 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. TDRDs have diverse biological functions and may contain one or more copies of the 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
                 ....*....|....*....|....*....|....*....|....*...
gi 967042226 769 ICAAP-GADGAWWRAQVVaSYEETNEVEIRYVDYGGYKRVKVDVLRQI 815
Cdd:cd20379    4 LCAAKyEEDGKWYRARVL-EVLSNDKVEVFFVDYGNTETVPLSDLRPL 50

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a 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 967042226 723 VNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPgIPTLPTPveiTVICAAPGADGA---WWRAQVVasYEETNEVEIRYV 799
Cdd:cd20431    4 VEVGHFWGYRIDENSSEILQQLTAEINQRQLVP-LTTKPVP---NLLCLAPFTDADmkkYYRAKIL--YVSGSSAEVFFV 77

                         90       100
                 ....*....|....*....|....
gi 967042226 800 DYGGYKRVKVDVLRQIRSDFVTLP 823
Cdd:cd20431   78 DYGNTSQVPSSLLREIPETLLTLP 101

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLI 676
Cdd:cd22439    5 EITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLI 65

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTlPYTQSVQIcHIEGSQHHVDKALNLI 676
Cdd:cd02394    5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPD-DEANSDEI-RIEGSPEGVKKAKAEI 63

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967042226 619 VPKHLVGRLIGKQGRYVSFLKQTSGAKIYIST---LPYTQSV--QICHIEGSQHHVDKALNLIGK 678
Cdd:cd22460    6 VASSQAGSLIGKGGAIIKQIREESGASVRILPeeeLPPCASPddRVVQISGEAQAVKKALELVSS 70

third 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 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
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 967042226 762 TPVEITVICAAPGADGAWWRAQVVASYEETNeVEIRYVDYGGYKRVKVDVLRQIRSDF 819
Cdd:cd20410    2 KPIVGEPCCAFFSGDGNWYRAMVKEILPGGA-VKVHFVDYGNVEEVTLDKLRKITSTF 58

fourth 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 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967042226 751 CYSQPGIPTL-PTPVEITviCAAPGADGAWWRAQVVASyeETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQ 825
Cdd:cd20411   37 CSKQSVPQQFrPRIGDAC--CARFTGDKNWYRAVVLET--SDSEVKVLYADYGNTETLPLSRILPITKSHLELPFQ 108

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967042226 617 IEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYIST----LPYTQSVQIChIEGSQHHVDKALNLIGKK 679
Cdd:cd22514    5 IGVPDEHIGAILGRGGRTINEIQQHSGARIKISDrgdfVSGTRNRKVT-ITGPQDAVQMAQYLLEQK 70

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967042226 623 LVGRLIGKQGRYVSFLKQTSGAKIYISTLpytQSVQICH------IEGSQHHVDKALNLIGKKFKE 682
Cdd:cd22494   10 LVGRLIGKEGRNLKKIEQDTGTKITISSL---QDLTIYNpertitVKGSIEACSSAEVEIMKKLRE 72

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGKK 679
Cdd:cd22522   12 ELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINAR 75

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967042226 618 EVP------KHLVGRLIGKQGRYVSFLKQTSGAKIYISTLP----YTQSVQIChIEGSQHHVDKALNLIGKKFKELNLTN 687
Cdd:cd22493    4 EVPlkilahNNFVGRLIGKEGRNLKKVEQDTETKITISPLQdltlYNPERTIT-VKGSIEACCRAEQEIMKKVREAYEND 82

                         90
                 ....*....|....
gi 967042226 688 IYAPPLPSLALPSL 701
Cdd:cd22493   83 VAAMNLQSHLIPGL 96

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYT--QSVQICHIEGSQHHVDKALNLI 676
Cdd:cd22463    5 EFQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYPleETQKILRISGTEEQLKRAQSLV 67

second 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 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.

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                 ....*....|....*....|....*....|....*....|....*....
gi 967042226 767 TVICAAPGADGAWWRAQVVASYEETNeVEIRYVDYGGYKRVKVDVLRQI 815
Cdd:cd20409   30 EVCCAQFTEDNQWYRASVLAYSSEDS-VLVGYIDFGNSEEVALSRLRPI 77

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLI 676
Cdd:cd22521    8 ELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLI 68

ribonuclease Y;

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967042226 307 SLDRNEENLDRNEESLDRNEEGLDRNEEGLDRNGEGLDRNEEIEQAAFQIISQV-ISEATEQVLATAVGKVT 377
Cdd:PRK00106 112 SLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALsQAEAREIILAETENKLT 183

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; 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. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967042226 616 EIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGK 678
Cdd:cd22480    4 EYKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQAKRLLGQ 66