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Conserved domains on  [gi|1907100828|ref|XP_036014465|]
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tudor domain-containing protein 3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
555-607 2.45e-32

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains 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: 410484  Cd Length: 53  Bit Score: 118.60  E-value: 2.45e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPV 607
Cdd:cd20413     1 WKPGDECLAKYWEDNKFYRAEVTAVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
RMI1_N super family cl07265
RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic ...
1-72 4.26e-21

RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic proteins. The domain probably carries an oligo-nucleotide-binding domain or OB-fold, and forms a stable complex with Bloom syndrome protein BLM and DNA topoisomerase 3-alpha.


The actual alignment was detected with superfamily member pfam08585:

Pssm-ID: 462527  Cd Length: 194  Bit Score: 91.56  E-value: 4.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907100828   1 MLRVQMTDGHTSCTAVEFSYISKISLNTPPGTKVKLSGTVDIKNGFLLLSDSNTTVLGGEVEHLIDKWALQR 72
Cdd:pfam08585 123 MLKLVLTDGGQKVYAIEYKPIPGLSLKLPPGTKLLLKGNVVVRRGVLLLTPENVKVLGGEVEELDKAWREGR 194
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
194-232 1.30e-17

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.


:

Pssm-ID: 270468  Cd Length: 39  Bit Score: 76.43  E-value: 1.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLLN 232
Cdd:cd14282     1 VDEKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT 39
 
Name Accession Description Interval E-value
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
555-607 2.45e-32

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains 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: 410484  Cd Length: 53  Bit Score: 118.60  E-value: 2.45e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPV 607
Cdd:cd20413     1 WKPGDECLAKYWEDNKFYRAEVTAVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
RMI1_N pfam08585
RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic ...
1-72 4.26e-21

RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic proteins. The domain probably carries an oligo-nucleotide-binding domain or OB-fold, and forms a stable complex with Bloom syndrome protein BLM and DNA topoisomerase 3-alpha.


Pssm-ID: 462527  Cd Length: 194  Bit Score: 91.56  E-value: 4.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907100828   1 MLRVQMTDGHTSCTAVEFSYISKISLNTPPGTKVKLSGTVDIKNGFLLLSDSNTTVLGGEVEHLIDKWALQR 72
Cdd:pfam08585 123 MLKLVLTDGGQKVYAIEYKPIPGLSLKLPPGTKLLLKGNVVVRRGVLLLTPENVKVLGGEVEELDKAWREGR 194
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
194-232 1.30e-17

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.


Pssm-ID: 270468  Cd Length: 39  Bit Score: 76.43  E-value: 1.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLLN 232
Cdd:cd14282     1 VDEKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT 39
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
555-606 7.22e-10

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 54.97  E-value: 7.22e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907100828  555 WKPGDECFAlYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNIKP 606
Cdd:smart00333   3 FKVGDKVAA-RWEDGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQ 52
TUDOR pfam00567
Tudor domain;
556-606 1.57e-08

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 53.13  E-value: 1.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNIKP 606
Cdd:pfam00567  49 AVGDGCVAAFSEDGKWYRAKITESLDDGL-VEVLFIDYGNTETVPLSDLRP 98
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
195-231 4.36e-06

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 43.63  E-value: 4.36e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907100828  195 DEKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
194-230 1.14e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 42.43  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVL 230
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
 
Name Accession Description Interval E-value
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
555-607 2.45e-32

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains 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: 410484  Cd Length: 53  Bit Score: 118.60  E-value: 2.45e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPV 607
Cdd:cd20413     1 WKPGDECLAKYWEDNKFYRAEVTAVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
RMI1_N pfam08585
RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic ...
1-72 4.26e-21

RecQ mediated genome instability protein; RMI1_N is an N-terminal family of eukaryotic proteins. The domain probably carries an oligo-nucleotide-binding domain or OB-fold, and forms a stable complex with Bloom syndrome protein BLM and DNA topoisomerase 3-alpha.


Pssm-ID: 462527  Cd Length: 194  Bit Score: 91.56  E-value: 4.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907100828   1 MLRVQMTDGHTSCTAVEFSYISKISLNTPPGTKVKLSGTVDIKNGFLLLSDSNTTVLGGEVEHLIDKWALQR 72
Cdd:pfam08585 123 MLKLVLTDGGQKVYAIEYKPIPGLSLKLPPGTKLLLKGNVVVRRGVLLLTPENVKVLGGEVEELDKAWREGR 194
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
194-232 1.30e-17

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.


Pssm-ID: 270468  Cd Length: 39  Bit Score: 76.43  E-value: 1.30e-17
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLLN 232
Cdd:cd14282     1 VDEKALRHITEMGFSKEAARQALMDNNNNLEAALNFLLT 39
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
558-607 3.70e-17

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single 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: 410549  Cd Length: 50  Bit Score: 75.37  E-value: 3.70e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907100828 558 GDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPV 607
Cdd:cd21182     1 GDKCLAPYSDDGKYYEATIEEITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
555-610 8.73e-12

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Overexpression of SPF30 causes apoptosis. It contains 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: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 60.40  E-value: 8.73e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSGmTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20399     1 WKVGDKCMAVWSEDGQYYEATIEEISEDG-TCTVTFDGYGNTEVTPLSQLKPREEG 55
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
556-610 1.44e-11

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.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 60.55  E-value: 1.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEAlHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20409    27 AVGEVCCAQFTEDNQWYRASVLA-YSSEDSVLVGYIDFGNSEEVALSRLRPIPPS 80
Tudor_SMN cd20398
Tudor domain found in survival motor neuron protein (SMN) and similar proteins; SMN, also ...
555-610 5.06e-10

Tudor domain found in survival motor neuron protein (SMN) and similar proteins; SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Mutations in human SMN lead to motor neuron degeneration and spinal muscular atrophy. SMN contains a central, highly conserved Tudor domain that is required for U snRNP assembly and Sm protein binding and has been shown to bind arginine-glycine-rich motifs in an methylarginine-dependent manner.


Pssm-ID: 410469  Cd Length: 56  Bit Score: 55.35  E-value: 5.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20398     1 WKVGDKCRAVYSEDGIIYEATIVSIDAERGTCVVRYTGYGNEEEQNLSDLLPPSGE 56
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
557-606 5.35e-10

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: 55.21  E-value: 5.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907100828 557 PGDECFALYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNIKP 606
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEVLSNDK-VEVFFVDYGNTETVPLSDLRP 49
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
555-606 7.22e-10

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 54.97  E-value: 7.22e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907100828  555 WKPGDECFAlYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNIKP 606
Cdd:smart00333   3 FKVGDKVAA-RWEDGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQ 52
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
558-606 2.06e-09

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 53.36  E-value: 2.06e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907100828 558 GDECFALYWEDNKFYRAEVEALHSSGmTAVVKFtDYGNYEEVLLSNIKP 606
Cdd:cd04508     1 GDRVEAKWSDDGQWYPATVVAVNDDG-KYTVLF-DDGNEEEVSEDDIRP 47
TUDOR pfam00567
Tudor domain;
556-606 1.57e-08

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 53.13  E-value: 1.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNIKP 606
Cdd:pfam00567  49 AVGDGCVAAFSEDGKWYRAKITESLDDGL-VEVLFIDYGNTETVPLSDLRP 98
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
558-610 1.51e-07

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.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 50.96  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 558 GDECFALYWEDNKFYRAEVEALHSSGMTavVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20426    50 GDPCIVKYSEDNHWYRALVTKINDNLVS--VRFVDYGNEEDVVREQVRALPSE 100
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
543-606 3.59e-07

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: 48.07  E-value: 3.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907100828 543 IESSIPVEYAKVWKPGDECFALYWEDNKFYRAEVEALhSSGMTAVVKFTDYGNYEEVLLSNIKP 606
Cdd:cd20433    16 IASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVEKV-EGDKKVHVLYIDYGNREVLPSTRLAA 78
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
556-607 5.39e-07

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.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 46.95  E-value: 5.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGmTAVVKFTDYGNYEEVLLSNIKPV 607
Cdd:cd20410     4 IVGEPCCAFFSGDGNWYRAMVKEILPGG-AVKVHFVDYGNVEEVTLDKLRKI 54
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
196-234 1.42e-06

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 45.16  E-value: 1.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNANNLEAALNVLLNSS 234
Cdd:cd14297     1 EDLVKQLVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
194-231 2.98e-06

UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270488 [Multi-domain]  Cd Length: 41  Bit Score: 44.30  E-value: 2.98e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:cd14303     1 VDPEALKQLTEMGFPEARATKALLLNRMSPTQAMEWLL 38
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
195-231 4.36e-06

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 43.63  E-value: 4.36e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907100828  195 DEKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:smart00165   1 DEEKIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
195-231 4.58e-06

UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270489  Cd Length: 39  Bit Score: 43.79  E-value: 4.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907100828 195 DEKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:cd14304     2 NPRAVQSLMEMGFEEEDVLEALRVTRNNQNAACEWLL 38
SMN pfam06003
Survival motor neuron protein (SMN); This family consists of several eukaryotic survival motor ...
553-614 6.19e-06

Survival motor neuron protein (SMN); This family consists of several eukaryotic survival motor neuron (SMN) proteins. The Survival of Motor Neurons (SMN) protein, the product of the spinal muscular atrophy-determining gene, is part of a large macromolecular complex (SMN complex) that functions in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). The SMN complex functions as a specificity factor essential for the efficient assembly of Sm proteins on U snRNAs and likely protects cells from illicit, and potentially deleterious, non-specific binding of Sm proteins to RNAs.


Pssm-ID: 428716 [Multi-domain]  Cd Length: 264  Bit Score: 48.07  E-value: 6.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907100828 553 KVWKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTEAWEE 614
Cdd:pfam06003  67 KEWKVGDSCNAFWSEDGNLYPATITSIDQKKGTCVVFYTGYGNEEEQNLADLLTPPPDMDED 128
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
199-228 6.48e-06

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 43.11  E-value: 6.48e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907100828 199 LKHITEMGFSKEASRQALMDNANNLEAALN 228
Cdd:cd14270     1 LAQLVEMGFSREQARRALRATNGDVEAAVE 30
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
543-606 6.77e-06

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: 45.82  E-value: 6.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907100828 543 IESSIPVEYAKV-----WKP--GDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKP 606
Cdd:cd20408    28 LTSQLKKTYASVnnhkeYIPevGEVCVAKYSEDQNWYRALVQTVDVQQKKAGVFYIDYGNEETVPLNRIQP 98
Tudor_SpSPF30-like cd20446
Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar ...
555-607 7.17e-06

Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. It contains 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: 410517  Cd Length: 56  Bit Score: 43.63  E-value: 7.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907100828 555 WKPGDECFAlYW--EDNKFYRAEVEALHSSGMTAV--VKFTDYGNYEEVLLSNIKPV 607
Cdd:cd20446     1 FKPGEVVMA-RWksGDGKFYPARITSITGSSINPIytVKFLDYGEIDTVYLKDIRPL 56
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
555-608 7.70e-06

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-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: 410471  Cd Length: 59  Bit Score: 43.47  E-value: 7.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907100828 555 WKPGDECFALYWEDNKFYRAEVEALHSSG---MTAVVKFTDYGNY--EEVLLSNIKPVQ 608
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDEngkSFAVVKFLGYESDedEKVPVSKLQKVK 59
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
556-610 1.06e-05

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.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 45.13  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVeaLHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20411    49 RIGDACCARFTGDKNWYRAVV--LETSDSEVKVLYADYGNTETLPLSRILPITKS 101
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
194-230 1.14e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 42.43  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVL 230
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGNNVERAAEYL 37
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
563-604 2.72e-05

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase 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: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 42.66  E-value: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907100828 563 ALYWEDNKFYRAEVEALHSSGMtAVVKFTDYGNYEEVLLSNI 604
Cdd:cd20430    27 GKFSEDNCWYRCKVKSILSDEK-CTVQYIDYGNTETVSRSSI 67
UBA_II_E2_pyUCE_like cd14314
UBA domain found in a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE) and ...
196-231 9.27e-05

UBA domain found in a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE) and similar proteins; P. Yoelii ubiquitin-conjugating enzyme and other uncharacterized family members show high sequence similarity to the human Huntingtin interacting protein-2 (HIP2) which belongs to a class II E2 ubiquitin-conjugating enzyme family. These proteins may play roles in the ubiquitin-mediated protein degradation pathway. They all contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain.


Pssm-ID: 270499  Cd Length: 37  Bit Score: 40.00  E-value: 9.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:cd14314     2 EEKIKKLLEMGFPRDQARKALEKNGWDETLALNTLL 37
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
194-231 9.31e-05

UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins; UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain.


Pssm-ID: 270490  Cd Length: 38  Bit Score: 40.02  E-value: 9.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:cd14305     1 PSEEQVQQLVDMGFSREDVLEALRQSNNDVNAATNLLL 38
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
561-613 1.26e-04

fifth 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 fifth 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: 410511  Cd Length: 127  Bit Score: 42.06  E-value: 1.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 561 CFALYWEDNKFYRAEVEALHSSGMTAVVkFTDYGNYEEVLLSNIKPVQTEAWE 613
Cdd:cd20440    63 CLAKYFEDGQWYRALAHPVESSSHLSVY-FVDYGNKQIVEKNEVLPIPDTAVD 114
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
196-233 1.84e-04

UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270484 [Multi-domain]  Cd Length: 38  Bit Score: 38.98  E-value: 1.84e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNANNLEAALNVLLNS 233
Cdd:cd14298     1 DEALAQLVSMGFDPEVARKALILTNGNVERAIEWLFSN 38
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
557-606 2.64e-04

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.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 40.45  E-value: 2.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 557 PGDECFALY--WEDNKFYRAEVeaLHSSGMTAVVKFTDYGNYEEV---LLSNIKP 606
Cdd:cd20431    43 PNLLCLAPFtdADMKKYYRAKI--LYVSGSSAEVFFVDYGNTSQVpssLLREIPE 95
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
556-605 5.02e-04

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.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 40.92  E-value: 5.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907100828 556 KPGDECFALYWEDNKFYRA---EVEALHSSgmtavVKFTDYGNYEEVLLSNIK 605
Cdd:cd20438    56 EPGLLCCARYSKDRHYYRAvitEVLDLKVS-----VYFLDFGNTDTVPFYDVK 103
UBA_TNR6C cd14283
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ...
197-231 5.61e-04

UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins; TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C.


Pssm-ID: 270469  Cd Length: 38  Bit Score: 37.87  E-value: 5.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907100828 197 KALKHITEMGFSKEASRQALMDNANNLEAALNVLL 231
Cdd:cd14283     2 RLLKQLTDMGFKREPAEEALKSNNMNLEQAVSALL 36
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
556-610 8.11e-04

sixth 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 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.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 39.34  E-value: 8.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGMTAvVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20441    39 KVGDLVAAEYDEDLALYRAVITAVLPGKSFK-VEFIDYGNTAVVDKSNIYTLQEK 92
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
556-605 8.39e-04

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.


Pssm-ID: 410513  Cd Length: 160  Bit Score: 40.41  E-value: 8.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIK 605
Cdd:cd20442    51 KEGLECLAKSKKNLKWYRAVVEHLYPETEKMLVFFVDHGITEVVSMGNIK 100
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
555-606 9.50e-04

fourth 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 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.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 39.78  E-value: 9.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907100828 555 WKPGD-ECFALYWEDNKFYRAEVEALHSSGMTAVVkFTDYGNYEEVLLSN---IKP 606
Cdd:cd20439    54 YKHGQiACVAKYSKDGKWYRAAVLKQVSAKEVDVI-FVDYGNQERVLISDlraIKP 108
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
202-232 1.12e-03

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 36.89  E-value: 1.12e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907100828 202 ITEMGFSKEASRQALMD-NANNLEAALNVLLN 232
Cdd:cd14327     6 LVEMGFSRERAEEALRAvGTNSVELAMEWLFT 37
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
194-232 1.60e-03

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 36.54  E-value: 1.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907100828 194 VDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLLN 232
Cdd:cd14386     1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVERAADWIFS 39
Tudor_PHF20-like cd20386
Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and ...
555-606 2.54e-03

Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and similar proteins; PHF20, also called Glioma-expressed antigen 2, hepatocellular carcinoma-associated antigen 58, novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds to Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53-mediated signaling. PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Both PHF20 and PHF20L1 contain an N-terminal malignant brain tumor (MBT) domain, a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410457 [Multi-domain]  Cd Length: 50  Bit Score: 36.42  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907100828 555 WKPGDECFAlYWEDNKFYRAEVEALHSSGmTAVVKFTDyGNYEEVLLSNIKP 606
Cdd:cd20386     1 FKVGEEVLA-RWSDCKFYPAKILKVLDNG-TYEVLFYD-GFKKTVKASNLKK 49
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
196-231 3.85e-03

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 3.85e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNAN-NLEAALNVLL 231
Cdd:cd14296     1 EEAVSQLMSMGFSENAAKRALYYTGNsSVEAAMNWLF 37
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
196-232 5.67e-03

UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p.


Pssm-ID: 270492  Cd Length: 38  Bit Score: 34.96  E-value: 5.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNANNLEAALNVLLN 232
Cdd:cd14307     1 EEAVASLLEMGIPREVAIEALRETNGDVEAAANYIFS 37
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
556-610 6.82e-03

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.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 35.92  E-value: 6.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 556 KPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20423     4 LPNPVCLAKYSEDGKWCRALIDNVYEPVEMVEVTYVDYGNKELVSLKNLRSISEE 58
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
195-228 7.40e-03

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 34.73  E-value: 7.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907100828 195 DEKALKHITEMGFSKEASRQALMDNANNLEAALN 228
Cdd:cd14291     1 DEDKLQQLMEMGFSEAEARLALRACNGNVERAVD 34
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
196-230 8.58e-03

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270570  Cd Length: 35  Bit Score: 34.27  E-value: 8.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907100828 196 EKALKHITEMGFSKEASRQALMDNANNLEAALNVL 230
Cdd:cd14387     1 EESIAILMSMGFPRNRAIEALKRTNNNLDRALDWL 35
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
556-610 9.15e-03

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.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 37.02  E-value: 9.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907100828 556 KPGDECfALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTE 610
Cdd:cd20421    62 KLGSPC-AARGSDGRWYRAVLQQVFSANRVVEVLHVDYGRKEVVSVSNLRYLAPE 115
 
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.
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