NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767908329|ref|XP_011507457|]
View 

tudor domain-containing protein 10 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD10 cd20432
Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 ...
 207-345 4.30e-91

Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm, and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and an RNA recognition motif (RRM). 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: 410503  Cd Length: 139  Bit Score: 270.07  E-value: 4.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329 207 LLRECFRDLSWLALIHSVRGEAGLLVTSIVPKTPFFWAMHVTEALHQNMQALFSTLAQAEEQQPYLEGSTVMRGTRCLAE 286
Cdd:cd20432    1 MLKDCFGDLSWLASIMKVHGEVGLLVTDTFPHTPYFWAILLTEESQQNMQQLFSTLAEVESQQPFLAKEDVHRGRRCLAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908329 287 YHLGDYGHAWNRCWVLDRVDTWAVVMFIDFGQLATIPVQSLRSLDSDDFWTIPPLTQPF 345
Cdd:cd20432   81 CPLGEEGGAWNRCWVLDVVEDFAVVFFVDFGSTANIPLPSLRSLDEDEFWQIPPLAQPF 139
RRM_TDRD10 cd21617
RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar ...
 42-135 6.89e-32

RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and a RNA recognition motif (RRM).


:

Pssm-ID: 410196 [Multi-domain]  Cd Length: 69  Bit Score: 114.82  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  42 EVYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPLDVHKIQNGCKCFAFVDLGSMQKVTLAIQE 121
Cdd:cd21617    1 EVYVGNLPLDIS-------------------------EEEILQLFKAFNPVLVKKIRSGFKCFAFVDLGSDENVKLAIQQ 55

                         90
                 ....*....|....
gi 767908329 122 LNGKLFHKRKLFVN 135
Cdd:cd21617   56 LNGTLFGGRRLVVN 69
 
Name Accession Description Interval E-value
Tudor_TDRD10 cd20432
Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 ...
 207-345 4.30e-91

Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm, and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and an RNA recognition motif (RRM). 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: 410503  Cd Length: 139  Bit Score: 270.07  E-value: 4.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329 207 LLRECFRDLSWLALIHSVRGEAGLLVTSIVPKTPFFWAMHVTEALHQNMQALFSTLAQAEEQQPYLEGSTVMRGTRCLAE 286
Cdd:cd20432    1 MLKDCFGDLSWLASIMKVHGEVGLLVTDTFPHTPYFWAILLTEESQQNMQQLFSTLAEVESQQPFLAKEDVHRGRRCLAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908329 287 YHLGDYGHAWNRCWVLDRVDTWAVVMFIDFGQLATIPVQSLRSLDSDDFWTIPPLTQPF 345
Cdd:cd20432   81 CPLGEEGGAWNRCWVLDVVEDFAVVFFVDFGSTANIPLPSLRSLDEDEFWQIPPLAQPF 139
RRM_TDRD10 cd21617
RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar ...
 42-135 6.89e-32

RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and a RNA recognition motif (RRM).


Pssm-ID: 410196 [Multi-domain]  Cd Length: 69  Bit Score: 114.82  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  42 EVYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPLDVHKIQNGCKCFAFVDLGSMQKVTLAIQE 121
Cdd:cd21617    1 EVYVGNLPLDIS-------------------------EEEILQLFKAFNPVLVKKIRSGFKCFAFVDLGSDENVKLAIQQ 55

                         90
                 ....*....|....
gi 767908329 122 LNGKLFHKRKLFVN 135
Cdd:cd21617   56 LNGTLFGGRRLVVN 69
RRM smart00360
RNA recognition motif;
43-134 1.75e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 45.28  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329    43 VYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPL-DVH----KIQNGCKCFAFVDLGSMQKVTL 117
Cdd:smart00360   2 LFVGNLPPDTT-------------------------EEELRELFSKFGKVeSVRlvrdKETGKSKGFAFVEFESEEDAEK 56

                           90
                   ....*....|....*..
gi 767908329   118 AIQELNGKLFHKRKLFV 134
Cdd:smart00360  57 ALEALNGKELDGRPLKV 73
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
44-143 7.44e-06

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


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 43.93  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  44 YVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNplDVHKIQ-------NGCKCFAFVDLGSMQKVT 116
Cdd:COG0724    5 YVGNLPYSVT-------------------------EEDLRELFSEYG--EVTSVKlitdretGRSRGFGFVEMPDDEEAQ 57

                         90       100
                 ....*....|....*....|....*..
gi 767908329 117 LAIQELNGKLFHKRKLFVNTSKRPPKR 143
Cdd:COG0724   58 AAIEALNGAELMGRTLKVNEARPREER 84
TUDOR pfam00567
Tudor domain;
251-347 1.28e-05

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 43.88  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  251 LHQNMQALFSTLAQaeeqqpylEGSTVMRGTRCLAEYHLGDyghAWNRCWVL-DRVDTWAVVMFIDFGQLATIPVQSLRS 329
Cdd:pfam00567  30 LTEELQEYYASKPP--------ESLPPAVGDGCVAAFSEDG---KWYRAKITeSLDDGLVEVLFIDYGNTETVPLSDLRP 98

                          90
                  ....*....|....*...
gi 767908329  330 LDSdDFWTIPPLTQPFML 347
Cdd:pfam00567  99 LPP-ELESLPPQAIKCQL 115
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 43-132 2.70e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 38.75  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329   43 VYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNP---LDVHKIQNG-CKCFAFV---DLGSMQKv 115
Cdd:pfam00076   1 LFVGNLPPDTT-------------------------EEDLKDLFSKFGPiksIRLVRDETGrSKGFAFVefeDEEDAEK- 54

                          90
                  ....*....|....*..
gi 767908329  116 tlAIQELNGKLFHKRKL 132
Cdd:pfam00076  55 --AIEALNGKELGGREL 69
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 102-154 2.80e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 2.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767908329  102 KCFAFVDLGSMQKVTLAIQELNGKLFHKRKLFVNTSKRPPKRTP---DMIQQPRAP 154
Cdd:TIGR01628 326 RGFGFVCFSNPEEANRAVTEMHGRMLGGKPLYVALAQRKEQRRAhlqDQFMQLQPR 381
 
Name Accession Description Interval E-value
Tudor_TDRD10 cd20432
Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 ...
 207-345 4.30e-91

Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm, and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and an RNA recognition motif (RRM). 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: 410503  Cd Length: 139  Bit Score: 270.07  E-value: 4.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329 207 LLRECFRDLSWLALIHSVRGEAGLLVTSIVPKTPFFWAMHVTEALHQNMQALFSTLAQAEEQQPYLEGSTVMRGTRCLAE 286
Cdd:cd20432    1 MLKDCFGDLSWLASIMKVHGEVGLLVTDTFPHTPYFWAILLTEESQQNMQQLFSTLAEVESQQPFLAKEDVHRGRRCLAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767908329 287 YHLGDYGHAWNRCWVLDRVDTWAVVMFIDFGQLATIPVQSLRSLDSDDFWTIPPLTQPF 345
Cdd:cd20432   81 CPLGEEGGAWNRCWVLDVVEDFAVVFFVDFGSTANIPLPSLRSLDEDEFWQIPPLAQPF 139
RRM_TDRD10 cd21617
RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar ...
 42-135 6.89e-32

RNA recognition motif (RRM) found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and a RNA recognition motif (RRM).


Pssm-ID: 410196 [Multi-domain]  Cd Length: 69  Bit Score: 114.82  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  42 EVYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPLDVHKIQNGCKCFAFVDLGSMQKVTLAIQE 121
Cdd:cd21617    1 EVYVGNLPLDIS-------------------------EEEILQLFKAFNPVLVKKIRSGFKCFAFVDLGSDENVKLAIQQ 55

                         90
                 ....*....|....
gi 767908329 122 LNGKLFHKRKLFVN 135
Cdd:cd21617   56 LNGTLFGGRRLVVN 69
RRM1_RRT5 cd12409
RNA recognition motif 1 (RRM1) found in yeast regulator of rDNA transcription protein 5 (RRT5) ...
 77-134 4.69e-07

RNA recognition motif 1 (RRM1) found in yeast regulator of rDNA transcription protein 5 (RRT5) and similar proteins; This subfamily corresponds to the RRM1 of the lineage specific family containing a group of uncharacterized yeast regulators of rDNA transcription protein 5 (RRT5), which may play roles in the modulation of rDNA transcription. RRT5 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains).


Pssm-ID: 409843 [Multi-domain]  Cd Length: 84  Bit Score: 47.27  E-value: 4.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767908329  77 SGEEEILYLLKDFNPLDV----HKIQNGCKCF------AFVDLGSMQKVTLAIQELNGKLFHKRKLFV 134
Cdd:cd12409   11 TTEEELEELLKDYKPVSVlipsYTVRGFRSRKhrplgiAYAEFSSVEEAEKVVKDLNGKVFKGRKLFV 78
RRM smart00360
RNA recognition motif;
43-134 1.75e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 45.28  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329    43 VYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPL-DVH----KIQNGCKCFAFVDLGSMQKVTL 117
Cdd:smart00360   2 LFVGNLPPDTT-------------------------EEELRELFSKFGKVeSVRlvrdKETGKSKGFAFVEFESEEDAEK 56

                           90
                   ....*....|....*..
gi 767908329   118 AIQELNGKLFHKRKLFV 134
Cdd:smart00360  57 ALEALNGKELDGRPLKV 73
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 43-135 3.76e-06

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).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 44.20  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  43 VYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNPLD----VHKIQNGCKCFAFVDLGSMQKVTLA 118
Cdd:cd00590    1 LFVGNLPPDTT-------------------------EEDLRELFSKFGEVVsvriVRDRDGKSKGFAFVEFESPEDAEKA 55

                         90
                 ....*....|....*..
gi 767908329 119 IQELNGKLFHKRKLFVN 135
Cdd:cd00590   56 LEALNGTELGGRPLKVS 72
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
44-143 7.44e-06

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


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 43.93  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  44 YVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNplDVHKIQ-------NGCKCFAFVDLGSMQKVT 116
Cdd:COG0724    5 YVGNLPYSVT-------------------------EEDLRELFSEYG--EVTSVKlitdretGRSRGFGFVEMPDDEEAQ 57

                         90       100
                 ....*....|....*....|....*..
gi 767908329 117 LAIQELNGKLFHKRKLFVNTSKRPPKR 143
Cdd:COG0724   58 AAIEALNGAELMGRTLKVNEARPREER 84
TUDOR pfam00567
Tudor domain;
251-347 1.28e-05

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 43.88  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329  251 LHQNMQALFSTLAQaeeqqpylEGSTVMRGTRCLAEYHLGDyghAWNRCWVL-DRVDTWAVVMFIDFGQLATIPVQSLRS 329
Cdd:pfam00567  30 LTEELQEYYASKPP--------ESLPPAVGDGCVAAFSEDG---KWYRAKITeSLDDGLVEVLFIDYGNTETVPLSDLRP 98

                          90
                  ....*....|....*...
gi 767908329  330 LDSdDFWTIPPLTQPFML 347
Cdd:pfam00567  99 LPP-ELESLPPQAIKCQL 115
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 280-330 1.29e-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: 42.12  E-value: 1.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767908329 280 GTRCLAEYHLGDyghAWNRCWVLDRV-DTWAVVMFIDFGQLATIPVQSLRSL 330
Cdd:cd20379    2 GDLCAAKYEEDG---KWYRARVLEVLsNDKVEVFFVDYGNTETVPLSDLRPL 50
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 43-132 2.70e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 38.75  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329   43 VYVGNLPLDISkagptcyltvkwaeepymwflqwsgEEEILYLLKDFNP---LDVHKIQNG-CKCFAFV---DLGSMQKv 115
Cdd:pfam00076   1 LFVGNLPPDTT-------------------------EEDLKDLFSKFGPiksIRLVRDETGrSKGFAFVefeDEEDAEK- 54

                          90
                  ....*....|....*..
gi 767908329  116 tlAIQELNGKLFHKRKL 132
Cdd:pfam00076  55 --AIEALNGKELGGREL 69
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 102-154 2.80e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 2.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767908329  102 KCFAFVDLGSMQKVTLAIQELNGKLFHKRKLFVNTSKRPPKRTP---DMIQQPRAP 154
Cdd:TIGR01628 326 RGFGFVCFSNPEEANRAVTEMHGRMLGGKPLYVALAQRKEQRRAhlqDQFMQLQPR 381
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 262-332 1.00e-03

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and 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.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 37.67  E-value: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767908329 262 LAQAEEQQPYLEGS-TVMRGTRCLAEYHLGDyghAWNRCWVLD-RVDTWAVVMFIDFGQLATIPVQSLRSLDS 332
Cdd:cd20433   12 LRFEIASNPPLPGSyTPRKGDLCAAKFVEDG---EWYRAKVEKvEGDKKVHVLYIDYGNREVLPSTRLAALPP 81
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 247-340 1.73e-03

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.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 38.12  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908329 247 VTEALHQNMQALFSTLAQAEEQQPYlegsTVMRGTRCLAEYHLGdygHAWNRCWV--LDRVDTWAVVMFIDFGQLATIPV 324
Cdd:cd20408   21 VLESLVKLTSQLKKTYASVNNHKEY----IPEVGEVCVAKYSED---QNWYRALVqtVDVQQKKAGVFYIDYGNEETVPL 93

                         90
                 ....*....|....*.
gi 767908329 325 QSLRSLDsDDFWTIPP 340
Cdd:cd20408   94 NRIQPLK-KDIELFPP 108
RRM1_CoAA cd12608
RNA recognition motif 1 (RRM1) found in vertebrate RRM-containing coactivator activator ...
 102-137 3.04e-03

RNA recognition motif 1 (RRM1) found in vertebrate RRM-containing coactivator activator/modulator (CoAA); This subgroup corresponds to the RRM1 of CoAA, also termed RNA-binding protein 14 (RBM14), or paraspeckle protein 2 (PSP2), or synaptotagmin-interacting protein (SYT-interacting protein), a heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein identified as a nuclear receptor coactivator. It mediates transcriptional coactivation and RNA splicing effects in a promoter-preferential manner and is enhanced by thyroid hormone receptor-binding protein (TRBP). CoAA contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a TRBP-interacting domain. It stimulates transcription through its interactions with coactivators, such as TRBP and CREB-binding protein CBP/p300, via the TRBP-interacting domain and interaction with an RNA-containing complex, such as DNA-dependent protein kinase-poly(ADP-ribose) polymerase complexes, via the RRMs.


Pssm-ID: 410020 [Multi-domain]  Cd Length: 69  Bit Score: 35.93  E-value: 3.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767908329 102 KCFAFVDLGSMQKVTLAIQELNGKLFHKRKLFVNTS 137
Cdd:cd12608   34 KQFAFVHMRGEAAADRAIRELNGRELHGRALVVEES 69
 
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