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Conserved domains on  [gi|1958652981|ref|XP_038956789|]
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putative ATP-dependent RNA helicase TDRD12 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 9-112 1.60e-61

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.


The actual alignment was detected with superfamily member cd20434:

Pssm-ID: 470623  Cd Length: 164  Bit Score: 207.28  E-value: 1.60e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981    9 VCVVYCQELKCWCRAVIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLYCTKPVTLHIDFCE 88
Cdd:cd20434     61 VCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCE 140

                           90       100
                   ....*....|....*....|....
gi 1958652981   89 DNAEIVPATKWDSAAIQYFQNILR 112
Cdd:cd20434    141 DKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 841-963 1.74e-42

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: 151.63  E-value: 1.74e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  841 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 909
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652981  910 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 963
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
364-788 2.04e-11

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 67.48  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  364 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 434
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  435 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 510
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  511 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 585
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  586 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 664
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  665 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 733
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652981  734 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 788
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1120-1195 5.73e-11

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


:

Pssm-ID: 107220  Cd Length: 84  Bit Score: 59.99  E-value: 5.73e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652981 1120 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1195
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 9-112 1.60e-61

first 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 first/N-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: 410505  Cd Length: 164  Bit Score: 207.28  E-value: 1.60e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981    9 VCVVYCQELKCWCRAVIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLYCTKPVTLHIDFCE 88
Cdd:cd20434     61 VCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCE 140

                           90       100
                   ....*....|....*....|....
gi 1958652981   89 DNAEIVPATKWDSAAIQYFQNILR 112
Cdd:cd20434    141 DKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 841-963 1.74e-42

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: 151.63  E-value: 1.74e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  841 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 909
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652981  910 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 963
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
364-788 2.04e-11

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 67.48  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  364 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 434
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  435 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 510
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  511 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 585
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  586 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 664
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  665 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 733
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652981  734 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 788
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1120-1195 5.73e-11

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 59.99  E-value: 5.73e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652981 1120 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1195
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
TUDOR pfam00567
Tudor domain;
9-75 1.77e-10

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 59.68  E-value: 1.77e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958652981    9 VCVVYCQElkCWCRAVIKSIIssaDHYLAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLY 75
Cdd:pfam00567   55 VAAFSEDG--KWYRAKITESL---DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 374-582 8.82e-10

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 59.76  E-value: 8.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  374 LKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 444
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  445 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 523
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652981  524 HVLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPHVV 582
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
TUDOR pfam00567
Tudor domain;
857-949 5.73e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.58  E-value: 5.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  857 YETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKTLFQRVQVLEASQKedtwglGSVLVKFIDEGRTKLITRDQLLLLP 936
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD------GLVEVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 1958652981  937 EKFHTLPPQAVEF 949
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEXDc smart00487
DEAD-like helicases superfamily;
431-583 3.63e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 3.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981   431 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 504
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981   505 LTYRSLLFLRLCHLVLDEVHVLF-FEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNRHIEHLVREFMKDPHVVI 583
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHRLLdGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 393-547 5.06e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.93  E-value: 5.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  393 SWPPIARGCDVVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 461
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  462 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHVLF---FEanEQMFAIL 538
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1958652981  539 DNFKKNVEV 547
Cdd:pfam00270  143 RRLPKKRQI 151
PTZ00424 PTZ00424
helicase 45; Provisional
 486-713 2.53e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  486 KLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEvhvlffeANEQM-----FAILDNFKK---NVEVEE-RESAPHQ 556
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE-------ADEMLsrgfkGQIYDVFKKlppDVQVALfSATMPNE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  557 IVavgvhwnrhieHLVREFMKDPHVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFVP-SQAqktLIFTCSVAET 635
Cdd:PTZ00424   215 IL-----------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKV 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  636 EIVCKVVESNSIFCLKMHKEMAFNLKSILeqwKKKLSSGSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVFGG 711
Cdd:PTZ00424   281 DYLTKKMHERDFTVSCMHGDMDQKDRDLI---MREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIH 353


                   ..
gi 1958652981  712 RL 713
Cdd:PTZ00424   354 RI 355
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 9-112 1.60e-61

first 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 first/N-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: 410505  Cd Length: 164  Bit Score: 207.28  E-value: 1.60e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981    9 VCVVYCQELKCWCRAVIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLYCTKPVTLHIDFCE 88
Cdd:cd20434     61 VCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCE 140

                           90       100
                   ....*....|....*....|....
gi 1958652981   89 DNAEIVPATKWDSAAIQYFQNILR 112
Cdd:cd20434    141 DKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 841-963 1.74e-42

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: 151.63  E-value: 1.74e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  841 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 909
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652981  910 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 963
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
364-788 2.04e-11

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 67.48  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  364 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 434
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  435 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 510
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  511 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 585
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  586 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 664
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  665 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 733
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652981  734 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 788
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1120-1195 5.73e-11

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 59.99  E-value: 5.73e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652981 1120 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1195
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
TUDOR pfam00567
Tudor domain;
9-75 1.77e-10

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 59.68  E-value: 1.77e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958652981    9 VCVVYCQElkCWCRAVIKSIIssaDHYLAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLY 75
Cdd:pfam00567   55 VAAFSEDG--KWYRAKITESL---DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1116-1220 3.89e-10

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 58.37  E-value: 3.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981 1116 PQIKWFQKDDHIILKIKIRNVKDYKCKFFTDRVIFSAWVG--DKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRA 1193
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958652981 1194 -CWCGLLKQ--RNPNVAFDFDHWeeCEEDS 1220
Cdd:cd06465     81 eYWPRLTKEkgKLPWLKVDFDKW--VDEDE 108
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 374-582 8.82e-10

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 59.76  E-value: 8.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  374 LKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 444
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  445 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 523
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652981  524 HVLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPHVV 582
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 431-584 8.37e-07

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 50.88  E-value: 8.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  431 KSLPSRNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKNmKLPRGCDVIVTTPHSLLRLLTYRSL 510
Cdd:cd17952     56 RELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKAT 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958652981  511 LFLRLCHLVLDEVHVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPhVVIT 584
Cdd:cd17952    134 NLQRVTYLVLDEADRMFdmgFEY--QVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDP-IRVV 197
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 8-56 1.06e-06

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: 46.74  E-value: 1.06e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958652981    8 KVCVVYCQELKCWCRAVIKSIISSadhYLAECFLVDFAKYIPVKSKNIR 56
Cdd:cd20379      3 DLCAAKYEEDGKWYRARVLEVLSN---DKVEVFFVDYGNTETVPLSDLR 48
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 438-583 1.30e-06

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 50.28  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  438 GPLAVIVCPGWKKAQFIFELLGDYSMSSrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCH 517
Cdd:cd17957     60 GLRALILAPTRELASQIYRELLKLSKGT-GLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEY 138

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652981  518 LVLDEVHVLF---F-EANEQMFAILDNFKKNVEVeerESA--PHQivavgvhwnrhIEHLVREFMKDPHVVI 583
Cdd:cd17957    139 LVLDEADKLFepgFrEQTDEILAACTNPNLQRSL---FSAtiPSE-----------VEELARSVMKDPIRII 196
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 3-75 1.81e-06

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: 47.09  E-value: 1.81e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652981    3 EVLVLKVCVVYCQELKCWCRAVIKSIISSADHylAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLY 75
Cdd:cd20423      2 HSLPNPVCLAKYSEDGKWCRALIDNVYEPVEM--VEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLY 72
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 356-578 2.09e-06

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 50.39  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  356 RNRIEPCLTLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPLLYLPPLLTI-------LQMGg 428
Cdd:cd18049     17 HNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVhinhqpfLERG- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  429 cykslpsrNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYR 508
Cdd:cd18049     96 --------DGPICLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAG 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652981  509 SLLFLRLCHLVLDEVHVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKD 578
Cdd:cd18049    166 KTNLRRCTYLVLDEADRMLdmgFEP--QIRKIVDQIRPD----------RQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 437-584 3.19e-06

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 49.63  E-value: 3.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  437 NGPLAVIVCPGWKKAQFI---FELLGDYsmssRPLhPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFL 513
Cdd:cd17945     65 DGPYALILAPTRELAQQIeeeTQKFAKP----LGI-RVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  514 RLCHLVLDEVHVLF---FEanEQMFAILDNFKKNVEVEERESAPHQiVAVGVHWNRH-----------IEHLVREFMKDP 579
Cdd:cd17945    140 QCTYVVLDEADRMIdmgFE--PQVTKILDAMPVSNKKPDTEEAEKL-AASGKHRYRQtmmftatmppaVEKIAKGYLRRP 216


                   ....*
gi 1958652981  580 hVVIT 584
Cdd:cd17945    217 -VVVT 220
TUDOR pfam00567
Tudor domain;
857-949 5.73e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.58  E-value: 5.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  857 YETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKTLFQRVQVLEASQKedtwglGSVLVKFIDEGRTKLITRDQLLLLP 936
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD------GLVEVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 1958652981  937 EKFHTLPPQAVEF 949
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEXDc smart00487
DEAD-like helicases superfamily;
431-583 3.63e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 3.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981   431 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 504
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981   505 LTYRSLLFLRLCHLVLDEVHVLF-FEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNRHIEHLVREFMKDPHVVI 583
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHRLLdGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 393-547 5.06e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.93  E-value: 5.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  393 SWPPIARGCDVVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 461
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  462 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHVLF---FEanEQMFAIL 538
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1958652981  539 DNFKKNVEV 547
Cdd:pfam00270  143 RRLPKKRQI 151
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 595-709 9.03e-05

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 43.65  E-value: 9.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  595 VQQVVHLCLECEKTSTLLQVLdFVPSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKkklsS 673
Cdd:cd18787      1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEErERALKKFR----S 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958652981  674 GSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVF 709
Cdd:cd18787     76 GKVRVLVATD----VAArgldIPGVDHVINYDLPRDAEDY 111
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 431-542 1.22e-04

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 44.64  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  431 KSLP--SRNGPLAVIVCPGWKKAQFIFELLGDY----SMSSRPLHPVLLTIG--LHKDEAKNMKlpRGCDVIVTTPHSLL 502
Cdd:cd17951     57 KKLPfiKGEGPYGLIVCPSRELARQTHEVIEYYckalQEGGYPQLRCLLCIGgmSVKEQLEVIR--KGVHIVVATPGRLM 134

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958652981  503 RLLTYRsLLFLRLC-HLVLDEVHVLF---FEanEQMFAILDNFK 542
Cdd:cd17951    135 DMLNKK-KINLDICrYLCLDEADRMIdmgFE--EDIRTIFSYFK 175
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 376-579 1.36e-04

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 44.28  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  376 KALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPllylppllTILQMggcyksLPS------------RNGPLAVI 443
Cdd:cd17966      3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGK--------TLAFL------LPAivhinaqpplerGDGPIVLV 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  444 VCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKnMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV 523
Cdd:cd17966     69 LAPTRELAQQIQQEANKFGGSSR-LRNTCVYGGAPKGPQI-RDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEA 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652981  524 HVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDP 579
Cdd:cd17966    147 DRMLdmgFEP--QIRKIVDQIRPD----------RQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 374-579 1.71e-04

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 44.11  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  374 LKKAL-QRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPllylppllT------ILQMGGCYKSLPSRN-GPLAVIVC 445
Cdd:cd17949      1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGK--------TlayllpIIQRLLSLEPRVDRSdGTLALVLV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  446 PGWKKAQFIFELLGDYSMSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLL-RLLTYRSLLFLRLCHLVLDEVH 524
Cdd:cd17949     73 PTRELALQIYEVLEKLLKPFHWIVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEAD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652981  525 VLF---FEAN-EQMFAILDNFKKNVEVEERESAPHQIVAVGVHWNRHIEHLVREFMKDP 579
Cdd:cd17949    152 RLLdmgFEKDiTKILELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 430-561 2.41e-04

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 43.89  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  430 YKSLPSR--NGPLAVIVCPGWKKAQFIFELLGDYSmSSRPLHPVLLTIGLHKdeaKNMKLPR--GCDVIVTTPHSLLRLL 505
Cdd:cd17948     55 YKLLAEGpfNAPRGLVITPSRELAEQIGSVAQSLT-EGLGLKVKVITGGRTK---RQIRNPHfeEVDILVATPGALSKLL 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652981  506 TYR--SLLFLRlcHLVLDEVHVLFFEA-NEQMFAILDNF---KKNVEVEERESAPHQIVAVG 561
Cdd:cd17948    131 TSRiySLEQLR--HLVLDEADTLLDDSfNEKLSHFLRRFplaSRRSENTDGLDPGTQLVLVS 190
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 1115-1215 3.34e-04

p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.


Pssm-ID: 107218  Cd Length: 106  Bit Score: 41.33  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981 1115 HPQIKWFQKDDHIILKIKIRNVKDYKCKFFTDRVIFSAWVGDKF-YLADMELQGDIRKDDCKCIIKDDEPLITLAK-EKR 1192
Cdd:cd00237      1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVkIYNEIELYDRVDPNDSKHKRTDRSILCCLRKgKEG 80

                           90       100
                   ....*....|....*....|....*
gi 1958652981 1193 ACWCGLLKQR-NPN-VAFDFDHWEE 1215
Cdd:cd00237     81 VAWPRLTKEKaKPNwLSVDFDNWRD 105
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 913-962 1.28e-03

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: 39.70  E-value: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958652981  913 SVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIE 962
Cdd:cd20418     34 KILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDSE 83
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 305-578 1.60e-03

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 41.92  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  305 RLTEKK-DCDEKNGCVKLLQFLNPDPLRADEiSDLHQLQKVKLGTLQPGVVLRnriePCLTLDKSPLSADLKKALQRNKF 383
Cdd:cd18050      8 RLRKKKwDLSELPKFEKNFYVEHPEVARMTQ-YDVEELRRKKEITIRGVGCPK----PVFAFHQANFPQYVMDVLLDQNF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  384 PGPSHTASYSWPPIARGCDVVVISHCGNDPLLYLPPLLTILQMGGCYksLPSRNGPLAVIVCPGWKKAQFIFELLGDYSM 463
Cdd:cd18050     83 KEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY--LERGDGPICLVLAPTRELAQQVQQVADDYGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  464 SSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEVHVLF---FEAneQMFAILDN 540
Cdd:cd18050    161 SSR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLdmgFEP--QIRKIVDQ 236

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958652981  541 FKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKD 578
Cdd:cd18050    237 IRPD----------RQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 461-527 2.22e-03

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 41.21  E-value: 2.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652981  461 YSMSSRPLHPVLLTIGLHK--DEAKNMKL----PRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEVHVLF 527
Cdd:cd17965    126 YSVLKKLSHTVKLGIKTFSsgFGPSYQRLqlafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLF 198
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 1120-1189 2.27e-03

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 37.95  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981 1120 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA---------WVGDKFYLaDMELQGDIRKDDCKCIIKDDEPLITLA 1188
Cdd:cd00298      1 WYQTDDEVVVTVDLPGVkkEDIKVEVEDNVLTISGkreeeeereRSYGEFER-SFELPEDVDPEKSKASLENGVLEITLP 79


                   .
gi 1958652981 1189 K 1189
Cdd:cd00298     80 K 80
PTZ00424 PTZ00424
helicase 45; Provisional
 486-713 2.53e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  486 KLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEvhvlffeANEQM-----FAILDNFKK---NVEVEE-RESAPHQ 556
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE-------ADEMLsrgfkGQIYDVFKKlppDVQVALfSATMPNE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  557 IVavgvhwnrhieHLVREFMKDPHVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFVP-SQAqktLIFTCSVAET 635
Cdd:PTZ00424   215 IL-----------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKV 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  636 EIVCKVVESNSIFCLKMHKEMAFNLKSILeqwKKKLSSGSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVFGG 711
Cdd:PTZ00424   281 DYLTKKMHERDFTVSCMHGDMDQKDRDLI---MREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIH 353


                   ..
gi 1958652981  712 RL 713
Cdd:PTZ00424   354 RI 355
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 837-943 3.65e-03

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: 38.57  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  837 FYISNATNyfgriIDKHVDLYETLNAEMNEYFKDPSNK------TAAEKVENLGLYgleektlfqRVQVLEASqkedtwG 910
Cdd:cd20441      5 FFIQLSED-----EKVILQLAEELNETSEKSRENAAVKlkvgdlVAAEYDEDLALY---------RAVITAVL------P 64

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958652981  911 LGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLP 943
Cdd:cd20441     65 GKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 858-946 3.72e-03

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: 38.18  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  858 ETLNAEMNEYFKDPSNKTA--AEKVENLGLYGLEEKTLFqRVQVLEASQKEdtwglgsVLVKFIDEGRTKLITRDQLLLL 935
Cdd:cd20427      1 EQMEDEMKEFYSKSSTAMClrSPSVGQLVAVKAEEDAWL-RAQVIEVEEDK-------VKVYYVDHGFSEVVERSKLFKL 72

                           90
                   ....*....|.
gi 1958652981  936 PEKFHTLPPQA 946
Cdd:cd20427     73 NKQFYSLPFQA 83
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 430-522 7.04e-03

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 39.10  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652981  430 YKSLPSRNGPLAVIVCPGWKKAQFIFELLGDY-SMSSRPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYR 508
Cdd:cd17960     55 RKANLKKGQVGALIISPTRELATQIYEVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRK 134

                           90
                   ....*....|....*.
gi 1958652981  509 SLL--FLRLCHLVLDE 522
Cdd:cd17960    135 ADKvkVKSLEVLVLDE 150
 
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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