NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24653610|ref|NP_610950|]
View 

tejas [Drosophila melanogaster]

Protein Classification

tudor domain-containing protein( domain architecture ID 11585251)

tudor domain-containing protein adopts a beta-barrel-like structure and may bind to proteins with dimethylated arginine or lysine residues, or to methylated histone tails to facilitate protein-protein interactions; similar to Caenorhabditis elegans protein tag-250

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 7-93 4.19e-35

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


:

Pssm-ID: 193586  Cd Length: 87  Bit Score: 126.84  E-value: 4.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   7 LSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWITAVATAKSAHIQ 86
Cdd:cd09972   1 LEEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 24653610  87 KLVRCQK 93
Cdd:cd09972  81 SLVAKQK 87
TUDOR super family cl26991
Tudor domain;
379-488 2.81e-07

Tudor domain;


The actual alignment was detected with superfamily member pfam00567:

Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 49.27  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   379 HNFNFWIYN-DDFKDYEAQFANMQTFYESSesKNYTMPLFLITTDhLCVVRCTSGWERAKVLGYRSSNNkmtIEVELVDI 457
Cdd:pfam00567  12 SPSTFYIQPkSDSKKLEKLTEELQEYYASK--PPESLPPAVGDGC-VAAFSEDGKWYRAKITESLDDGL---VEVLFIDY 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 24653610   458 GDIIRVSQQNVKFLIKPFALLPRQCLAGRLA 488
Cdd:pfam00567  86 GNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
 
Name Accession Description Interval E-value
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 7-93 4.19e-35

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193586  Cd Length: 87  Bit Score: 126.84  E-value: 4.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   7 LSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWITAVATAKSAHIQ 86
Cdd:cd09972   1 LEEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 24653610  87 KLVRCQK 93
Cdd:cd09972  81 SLVAKQK 87
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 14-75 3.27e-12

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 61.80  E-value: 3.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653610    14 VHSLVVSSP-GKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWIT 75
Cdd:pfam12872   2 LISLLRSDPdGWASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
TUDOR pfam00567
Tudor domain;
379-488 2.81e-07

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 49.27  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   379 HNFNFWIYN-DDFKDYEAQFANMQTFYESSesKNYTMPLFLITTDhLCVVRCTSGWERAKVLGYRSSNNkmtIEVELVDI 457
Cdd:pfam00567  12 SPSTFYIQPkSDSKKLEKLTEELQEYYASK--PPESLPPAVGDGC-VAAFSEDGKWYRAKITESLDDGL---VEVLFIDY 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 24653610   458 GDIIRVSQQNVKFLIKPFALLPRQCLAGRLA 488
Cdd:pfam00567  86 GNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 374-487 4.56e-06

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS 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.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 45.90  E-value: 4.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610 374 SLVNPHNFNFWIY-NDDFKDYEAQFANMQTFYESSE-SKNYTMPLFLITTDHLCVVRCTSG--WERAKVlgyRSSNNKMT 449
Cdd:cd20419   4 YIESPSQFYVRFYsKDTSEMLEDMMIEMRRCYSNEHvSERYVMPEAFIQPGQVCCVRIPEDvwWYRVII---HQVLNKQE 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24653610 450 IEVELVDIGDIIRVSQQNVKFLIKPFALLPRQCLAGRL 487
Cdd:cd20419  81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
 
Name Accession Description Interval E-value
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 7-93 4.19e-35

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193586  Cd Length: 87  Bit Score: 126.84  E-value: 4.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   7 LSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWITAVATAKSAHIQ 86
Cdd:cd09972   1 LEEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 24653610  87 KLVRCQK 93
Cdd:cd09972  81 SLVAKQK 87
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 14-75 3.27e-12

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 61.80  E-value: 3.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653610    14 VHSLVVSSP-GKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWIT 75
Cdd:pfam12872   2 LISLLRSDPdGWASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
LOTUS_1_TDRD5 cd09985
The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on ...
 7-96 2.66e-11

The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193599  Cd Length: 95  Bit Score: 60.17  E-value: 2.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   7 LSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTV-TGHGQMAWITAVATAKSAHI 85
Cdd:cd09985   5 MERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVhPQLDGTVILKAVGDETTKGI 84

                        90
                ....*....|.
gi 24653610  86 QKLVRCQKKSK 96
Cdd:cd09985  85 EDLVSKQRDSK 95
LOTUS cd08824
LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and ...
 7-76 5.00e-10

LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7; LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7. The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation. Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. Limkain b1 contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193585 [Multi-domain]  Cd Length: 70  Bit Score: 55.70  E-value: 5.00e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   7 LSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWITA 76
Cdd:cd08824   1 LKQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIVSL 70
LOTUS_1_TDRD7 cd09986
The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on ...
 9-93 2.72e-09

The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193600  Cd Length: 88  Bit Score: 54.04  E-value: 2.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   9 LVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTgHGQMAWITAVATA--KSAHIQ 86
Cdd:cd09986   3 LVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLE-RSRSGEVMCFASLcnETAHIA 81


                ....*..
gi 24653610  87 KLVRCQK 93
Cdd:cd09986  82 KLVARQR 88
TUDOR pfam00567
Tudor domain;
379-488 2.81e-07

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 49.27  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610   379 HNFNFWIYN-DDFKDYEAQFANMQTFYESSesKNYTMPLFLITTDhLCVVRCTSGWERAKVLGYRSSNNkmtIEVELVDI 457
Cdd:pfam00567  12 SPSTFYIQPkSDSKKLEKLTEELQEYYASK--PPESLPPAVGDGC-VAAFSEDGKWYRAKITESLDDGL---VEVLFIDY 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 24653610   458 GDIIRVSQQNVKFLIKPFALLPRQCLAGRLA 488
Cdd:pfam00567  86 GNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 374-487 4.56e-06

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS 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.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 45.90  E-value: 4.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610 374 SLVNPHNFNFWIY-NDDFKDYEAQFANMQTFYESSE-SKNYTMPLFLITTDHLCVVRCTSG--WERAKVlgyRSSNNKMT 449
Cdd:cd20419   4 YIESPSQFYVRFYsKDTSEMLEDMMIEMRRCYSNEHvSERYVMPEAFIQPGQVCCVRIPEDvwWYRVII---HQVLNKQE 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24653610 450 IEVELVDIGDIIRVSQQNVKFLIKPFALLPRQCLAGRL 487
Cdd:cd20419  81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 419-522 1.16e-05

first 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 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.


Pssm-ID: 410507  Cd Length: 147  Bit Score: 45.49  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610 419 ITTDHLCVV--RCTSGWERAKVLGYRSSNnkmtIEVELVDIGDIIRVSQQNVKFLIKPFALLPRQCLAGRLAFITQCKSp 496
Cdd:cd20436  47 WGVGEFCLVedTTSGEWYRGRVLEKIDEK----YEVFLIDRGEVLNVHATNMASASGELFQLPPKAVCGIFANILPIGE- 121

                        90       100
                ....*....|....*....|....*.
gi 24653610 497 NWTAEVVNFFHDMILLRLLYAkVEAI 522
Cdd:cd20436 122 KWSSTAVNYFSSLIGSQVKGY-IQAI 146
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 422-471 3.00e-05

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.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 41.35  E-value: 3.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24653610 422 DHLCVVRCTSG--WERAKVLGYRSSNnkmTIEVELVDIGDIIRVSQQNVKFL 471
Cdd:cd20379   2 GDLCAAKYEEDgkWYRARVLEVLSND---KVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 398-490 9.18e-05

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five 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.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 41.65  E-value: 9.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653610 398 ANMQTFYESSESKNytMPLFLITTDHLCVVRCTSG-WERAKVLGYRSSNNkmtIEVELVDIGDIIRVSQQNVKFLIKPFA 476
Cdd:cd20415   6 KKIQEFYKEGDDGG--LEILCPVQGQACVALFEDGaWYRARIIGLPGHRE---VEVKYVDFGNTATVTIKHVRKIKDDFL 80

                        90
                ....*....|....
gi 24653610 477 LLPRQCLAGRLAFI 490
Cdd:cd20415  81 SLPEKARECRLAFI 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH