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Conserved domains on  [gi|568980584|ref|XP_006516384|]
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ATP-dependent RNA helicase TDRD9 isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 505-605 3.93e-55

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: 186.05  E-value: 3.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 505 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 584
Cdd:cd20431    1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                         90       100
                 ....*....|....*....|.
gi 568980584 585 NRSHVDLDLLREIPCQFLELP 605
Cdd:cd20431   81 NTSQVPSSLLREIPETLLTLP 101
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
2-305 2.03e-48

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 186.05  E-value: 2.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   2 HELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLR 81
Cdd:COG1643  237 AEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLP 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  82 LSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSD 161
Cdd:COG1643  317 TERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARA 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 162 IERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNfftmPFR 241
Cdd:COG1643  394 IADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRR 459

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980584 242 QhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwgRLNYIQIKRIREVAE 305
Cdd:COG1643  460 G-------------AAGSDLLARLNLWRRLREQQRE-------------FLSYLRLREWRDLAR 497
 
Name Accession Description Interval E-value
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 505-605 3.93e-55

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: 186.05  E-value: 3.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 505 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 584
Cdd:cd20431    1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                         90       100
                 ....*....|....*....|.
gi 568980584 585 NRSHVDLDLLREIPCQFLELP 605
Cdd:cd20431   81 NTSQVPSSLLREIPETLLTLP 101
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
2-305 2.03e-48

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 186.05  E-value: 2.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   2 HELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLR 81
Cdd:COG1643  237 AEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLP 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  82 LSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSD 161
Cdd:COG1643  317 TERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARA 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 162 IERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNfftmPFR 241
Cdd:COG1643  394 IADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRR 459

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980584 242 QhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwgRLNYIQIKRIREVAE 305
Cdd:COG1643  460 G-------------AAGSDLLARLNLWRRLREQQRE-------------FLSYLRLREWRDLAR 497
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 1-108 3.02e-48

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 169.25  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   1 MHELLTNMIH----KRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTN 76
Cdd:cd18791   59 LCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTG 138

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568980584  77 YQSLRLSWASKTSCDQRKGRAGRVSKGYCYRL 108
Cdd:cd18791  139 LSSLVTVWISKASAEQRAGRAGRTRPGKCYRL 170
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 14-336 4.55e-37

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 151.75  E-value: 4.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   14 QVYPLHSSVTLEEQNNVFLSPvpGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQR 93
Cdd:PRK11131  315 EILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQR 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   94 KGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVG 173
Cdd:PRK11131  393 KGRCGRVSEGICIRLYSEDDFLSR-PEFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELG 469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  174 ALavsgqREDENPHDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPF--RQHLDGYRNKV 251
Cdd:PRK11131  470 AI-----TTDEQASAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRF 544

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  252 HfsgSSRSDCLALVEAFRAWQAcrQRGELR----RPKDELDWgrLNYIqikRIREVAELYEELKNRISQFNMfvgphhPV 327
Cdd:PRK11131  545 A---DKESDFLAFVNLWNYLQE--QQKALSsnqfRRLCRTDY--LNYL---RVREWQDIYTQLRQVVKELGI------PV 608


                  ....*....
gi 568980584  328 LDQEYPYKQ 336
Cdd:PRK11131  609 NSEPAEYRE 617
TUDOR pfam00567
Tudor domain;
504-613 2.41e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 75.85  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  504 VTEVVEVGHFWgyRIDERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDynKESYFRAQILY-VSGNSAEVFF 580
Cdd:pfam00567   7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568980584  581 VDYGNRSHVDLDLLREIPCQFLELPFQALEFKI 613
Cdd:pfam00567  83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 188-265 3.30e-16

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 74.23  E-value: 3.30e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980584   188 DGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHfsgSSRSDCLALV 265
Cdd:smart00847   8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRRFA---DPESDHLTLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 166-246 9.99e-16

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 73.81  E-value: 9.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  166 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLD 245
Cdd:pfam04408   2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPR 71


                  .
gi 568980584  246 G 246
Cdd:pfam04408  72 S 72
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 550-601 1.63e-07

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: 48.81  E-value: 1.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568980584   550 VCLAPFTDYNkesYFRAQILYVSGN-SAEVFFVDYGNRSHVDLDLLREIPCQF 601
Cdd:smart00333   8 KVAARWEDGE---WYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
 
Name Accession Description Interval E-value
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 505-605 3.93e-55

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: 186.05  E-value: 3.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 505 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 584
Cdd:cd20431    1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                         90       100
                 ....*....|....*....|.
gi 568980584 585 NRSHVDLDLLREIPCQFLELP 605
Cdd:cd20431   81 NTSQVPSSLLREIPETLLTLP 101
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
2-305 2.03e-48

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 186.05  E-value: 2.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   2 HELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLR 81
Cdd:COG1643  237 AEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLP 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  82 LSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSD 161
Cdd:COG1643  317 TERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARA 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 162 IERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNfftmPFR 241
Cdd:COG1643  394 IADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRR 459

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980584 242 QhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwgRLNYIQIKRIREVAE 305
Cdd:COG1643  460 G-------------AAGSDLLARLNLWRRLREQQRE-------------FLSYLRLREWRDLAR 497
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 1-108 3.02e-48

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 169.25  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   1 MHELLTNMIH----KRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTN 76
Cdd:cd18791   59 LCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTG 138

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568980584  77 YQSLRLSWASKTSCDQRKGRAGRVSKGYCYRL 108
Cdd:cd18791  139 LSSLVTVWISKASAEQRAGRAGRTRPGKCYRL 170
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 14-336 4.55e-37

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 151.75  E-value: 4.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   14 QVYPLHSSVTLEEQNNVFLSPvpGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQR 93
Cdd:PRK11131  315 EILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQR 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   94 KGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVG 173
Cdd:PRK11131  393 KGRCGRVSEGICIRLYSEDDFLSR-PEFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELG 469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  174 ALavsgqREDENPHDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPF--RQHLDGYRNKV 251
Cdd:PRK11131  470 AI-----TTDEQASAYKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRF 544

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  252 HfsgSSRSDCLALVEAFRAWQAcrQRGELR----RPKDELDWgrLNYIqikRIREVAELYEELKNRISQFNMfvgphhPV 327
Cdd:PRK11131  545 A---DKESDFLAFVNLWNYLQE--QQKALSsnqfRRLCRTDY--LNYL---RVREWQDIYTQLRQVVKELGI------PV 608


                  ....*....
gi 568980584  328 LDQEYPYKQ 336
Cdd:PRK11131  609 NSEPAEYRE 617
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 2-201 1.18e-18

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 91.52  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   2 HELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSL- 80
Cdd:PRK11664 229 QEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLv 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  81 --RLSWASKTscdQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLGSTILkvKLLDMGEPRALLATALSPPS 158
Cdd:PRK11664 309 tqRISQASMT---QRAGRAGRLEPGICLHLYSKEQAERA-AAQSEPEILHSDLSGLLL--ELLQWGCHDPAQLSWLDQPP 382

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568980584 159 LSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQL 201
Cdd:PRK11664 383 AAALAAAKRLLQQLGALDGQGR----------LTARGRKMAAL 415
TUDOR pfam00567
Tudor domain;
504-613 2.41e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 75.85  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  504 VTEVVEVGHFWgyRIDERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDynKESYFRAQILY-VSGNSAEVFF 580
Cdd:pfam00567   7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568980584  581 VDYGNRSHVDLDLLREIPCQFLELPFQALEFKI 613
Cdd:pfam00567  83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 188-265 3.30e-16

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 74.23  E-value: 3.30e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980584   188 DGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHfsgSSRSDCLALV 265
Cdd:smart00847   8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRRFA---DPESDHLTLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 166-246 9.99e-16

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 73.81  E-value: 9.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584  166 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLD 245
Cdd:pfam04408   2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPR 71


                  .
gi 568980584  246 G 246
Cdd:pfam04408  72 S 72
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 504-630 3.54e-13

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


Pssm-ID: 410493  Cd Length: 135  Bit Score: 67.54  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 504 VTEVVEVGHFWgYRIDERN---AELLKQLTA---EINRLELVPLpiHPHPDLVCLAPFTDynkESYFRAQILYVSGNSAE 577
Cdd:cd20422    6 VEFVKDPSEFW-IRLGEHAvpfSKLMRSMTAfysQASKLDGVVL--KPQPGQLCCAKWKE---DRYYRAIVTAVKGKMVE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568980584 578 VFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPsaksliCGEHWS 630
Cdd:cd20422   80 VFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP------LGERWS 126
HELICc smart00490
helicase superfamily c-terminal domain;
3-99 6.06e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 62.23  E-value: 6.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584     3 ELLTNMIHKR-LQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLtrtlvcdedtnyqslr 81
Cdd:smart00490   1 EELAELLKELgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL---------------- 64

                           90
                   ....*....|....*...
gi 568980584    82 lsWASKTSCDQRKGRAGR 99
Cdd:smart00490  65 --PWSPASYIQRIGRAGR 80
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 520-613 3.59e-11

fifth 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 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: 410495  Cd Length: 126  Bit Score: 61.37  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 520 ERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDYNkesYFRAQILYVSgNSAEVFFVDYGNRSHVDLDLLREI 597
Cdd:cd20424   32 ARNAGVLDQLASAISRLssEIRKLELSVNPGTLCLAKYSDQH---WYRGIIITNK-NSTEVFFVDYGNTEKVEKEDMLPI 107

                         90
                 ....*....|....*....
gi 568980584 598 P---CQFLELPFQALEFKI 613
Cdd:cd20424  108 PsdaYELLLLPMQAIKCSL 126
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 541-610 3.41e-10

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


Pssm-ID: 410478  Cd Length: 76  Bit Score: 57.22  E-value: 3.41e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980584 541 LPIHPHPDLVCLAPFTDynkeSYFRAQILYVSG--NSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 610
Cdd:cd20407    1 LPEPIEVGVICAAPVMN----AWYRAQVVGVFEetDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATE 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 11-100 4.87e-10

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 57.61  E-value: 4.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   11 KRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLvcdedtnyqslrlswaskTSC 90
Cdd:pfam00271  37 EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNP------------------ASY 98

                          90
                  ....*....|
gi 568980584   91 DQRKGRAGRV 100
Cdd:pfam00271  99 IQRIGRAGRA 108
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 523-602 2.52e-09

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: 54.77  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 523 AELLKQLTAEINRLELVPLpIHPHPDLVCLAPFTDYNkeSYFRAQIL-YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQF 601
Cdd:cd20409    5 AELQESLSAYCKVAPASSD-FSPAVGEVCCAQFTEDN--QWYRASVLaYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSL 81


                 .
gi 568980584 602 L 602
Cdd:cd20409   82 L 82
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 547-597 5.46e-09

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: 52.90  E-value: 5.46e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568980584 547 PDLVCLAPFTDYNKesYFRAQILYV-SGNSAEVFFVDYGNRSHVDLDLLREI 597
Cdd:cd20379    1 VGDLCAAKYEEDGK--WYRARVLEVlSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 504-607 1.05e-08

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: 53.99  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 504 VTEVVEVGHFWGYRIDER-NAELLKQLTAEINRL---ELVPLPIHPHPDLVCLAPFTDYNkeSYFRAQILYVSGNSAEVF 579
Cdd:cd20411    3 VLEVISPDLFYALPKTGQvNVEKLKALMTELAEYcskQSVPQQFRPRIGDACCARFTGDK--NWYRAVVLETSDSEVKVL 80

                         90       100
                 ....*....|....*....|....*...
gi 568980584 580 FVDYGNRSHVDLDLLREIPCQFLELPFQ 607
Cdd:cd20411   81 YADYGNTETLPLSRILPITKSHLELPFQ 108
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 491-614 2.09e-08

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: 53.65  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 491 RPRTVADllltIDVTEVVEVGHFWGYRidERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKesYFRAQIL- 569
Cdd:cd20439    7 KPGSVVD----VKCSYVNSPGDFWCQL--QTKSSELKSLMKQIQSYYLIHNDPYKHGQIACVAKYSKDGK--WYRAAVLk 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568980584 570 YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQAleFKIC 614
Cdd:cd20439   79 QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQA--FRCS 121
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 548-618 4.22e-08

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal 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: 410506  Cd Length: 134  Bit Score: 53.02  E-value: 4.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980584 548 DLVCLapftDYNKESYFRAQILYVSGNS-------AEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 618
Cdd:cd20435   54 DLCAV----EDENNLYHRVKVLEITEKDdktkpreVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKP 127
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 548-610 4.97e-08

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


Pssm-ID: 410483  Cd Length: 95  Bit Score: 51.53  E-value: 4.97e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980584 548 DLVClAPFTDYNkeSYFRAQILYVSGNS-AEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 610
Cdd:cd20412   33 DIVA-APFRHDG--SWYRARVLGFLENGnLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIE 93
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 547-623 5.01e-08

fifth 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 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: 410489  Cd Length: 105  Bit Score: 52.03  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 547 PDLVCLAPFTDynkESYFRAQILYVSG-NSAEVF--FVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPSAKSL 623
Cdd:cd20418    6 PEMPCLAEYSD---GKWYRAKLLSILEfNPVKILvrHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDS 82
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 550-601 1.63e-07

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: 48.81  E-value: 1.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568980584   550 VCLAPFTDYNkesYFRAQILYVSGN-SAEVFFVDYGNRSHVDLDLLREIPCQF 601
Cdd:smart00333   8 KVAARWEDGE---WYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 504-611 2.88e-07

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: 50.15  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 504 VTEVVEVGHFwgYRIDERNAELLKQLTAEINrlELVPLPIHPHPDL----VCLAPFtdYNKESYFRAQILYVSGNS-AEV 578
Cdd:cd20440   16 ITHVYSPAKF--YCQLDRNTEILEALMEKIA--EISKLFNSQILDNcktrLCLAKY--FEDGQWYRALAHPVESSShLSV 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568980584 579 FFVDYGNRSHVDLDLLREIPCQFLEL---PFQALEF 611
Cdd:cd20440   90 YFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKC 125
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 544-610 4.26e-07

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: 48.25  E-value: 4.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980584 544 HPHPDLVCLAPFTDYNKesYFRAQILYVSGN--SAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 610
Cdd:cd20423    2 HSLPNPVCLAKYSEDGK--WCRALIDNVYEPveMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFR 68
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 545-618 1.38e-06

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: 47.43  E-value: 1.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980584 545 PHPDLVCLAPFTDYNkesYFRAQILYVSGNSA-EVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 618
Cdd:cd20415   25 PVQGQACVALFEDGA---WYRARIIGLPGHREvEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 545-602 1.51e-06

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: 46.18  E-value: 1.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568980584 545 PHPDLVCLAPFTDYNkeSYFRAQILYV-SGNSAEVFFVDYGNRSHVDLDLLREIPCQFL 602
Cdd:cd20410    3 PIVGEPCCAFFSGDG--NWYRAMVKEIlPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 561-618 1.56e-06

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The 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: 410498  Cd Length: 98  Bit Score: 47.42  E-value: 1.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568980584 561 ESYFRAQILYVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 618
Cdd:cd20427   36 DAWLRAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLAGLEP 93
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 9-106 7.49e-06

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 49.98  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584   9 IHKRLQVYPLHSSVTLEEQ--NNVFLSPVPgyrKIILSTNIAESSVTVPDVKYVIDfcLTRTLVCDEDTNYQSLrlswAS 86
Cdd:PHA02653 418 RLPIYDFYIIHGKVPNIDEilEKVYSSKNP---SIIISTPYLESSVTIRNATHVYD--TGRVYVPEPFGGKEMF----IS 488

                         90       100
                 ....*....|....*....|.
gi 568980584  87 KTSCDQRKGRAGRVSKG-YCY 106
Cdd:PHA02653 489 KSMRTQRKGRVGRVSPGtYVY 509
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 504-609 1.32e-05

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: 45.93  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 504 VTEVVEVGHFWgYRIDERNAE---LLKQLTAEINRLELVPLPIH-PHPDLVCLApftDYNKES-YFRAQILYVSGNSAEV 578
Cdd:cd20438   11 VEYVLNPSNFW-IRTDEYNNEfqaLMKNIADIYNLCGNDEELLKkPEPGLLCCA---RYSKDRhYYRAVITEVLDLKVSV 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568980584 579 FFVDYGNRSHVDLDLLREIPCQFLELPFQAL 609
Cdd:cd20438   87 YFLDFGNTDTVPFYDVKTLLPEFSELPALAM 117
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 523-601 6.15e-05

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: 42.29  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 523 AELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNkeSYFRAQILYVSGNS-AEVFFVDYGNRSHVDLDLLREIPCQF 601
Cdd:cd20433    6 EKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDG--EWYRAKVEKVEGDKkVHVLYIDYGNREVLPSTRLAALPPAF 83
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 512-641 1.81e-04

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: 42.49  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 512 HFWgYRIDERNAELLKQLTAEINRLELVPLPIHPHPDL--VCLAPFTDYNKesYFRAQILYVSGNSAEVFFVDYGNRSHV 589
Cdd:cd20426   13 YFW-CQFATEKIQCLAVKVQEAGEQVADRGNFIPSIYVgdPCIVKYSEDNH--WYRALVTKINDNLVSVRFVDYGNEEDV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568980584 590 DLDLLREIPCQFLELPFQALEFKICKMRPSAKSlicgehWSGGAHGRFAALV 641
Cdd:cd20426   90 VREQVRALPSELLKIPVQAFPCCLSGFNLSEGL------WSDEANDYFYEIV 135
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 548-605 2.83e-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: 41.26  E-value: 2.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568980584 548 DLVcLAPFTDYNkeSYFRAQIL-YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELP 605
Cdd:cd20441   42 DLV-AAEYDEDL--ALYRAVITaVLPGKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 551-597 1.31e-03

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: 37.71  E-value: 1.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568980584 551 CLAPFTDYNKesYFRAQI--LYVSGNSAEVFFVDYGNRSHVDLDLLREI 597
Cdd:cd20413    7 CLAKYWEDNK--FYRAEVtaVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 504-618 1.92e-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: 39.28  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980584 504 VTEVVEVGHFWGYRIDERNAELLKQLTAEinrLELVPLPIHPHPDL------VCLAPFT-DYNkesYFRAQILYVSGN-- 574
Cdd:cd20408    3 VTEFKNPGEFYIQIYTLEVLESLVKLTSQ---LKKTYASVNNHKEYipevgeVCVAKYSeDQN---WYRALVQTVDVQqk 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568980584 575 SAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 618
Cdd:cd20408   77 KAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKP 120
 
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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