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Conserved domains on  [gi|1958652984|ref|XP_038956790|]
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putative ATP-dependent RNA helicase TDRD12 isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 733-855 8.20e-43

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: 152.40  E-value: 8.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  733 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 801
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652984  802 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 855
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
256-680 1.82e-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: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  256 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 326
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  327 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 402
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  403 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 477
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  478 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 556
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  557 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 625
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652984  626 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 680
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1012-1087 4.47e-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: 4.47e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652984 1012 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1087
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 733-855 8.20e-43

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: 152.40  E-value: 8.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  733 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 801
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652984  802 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 855
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
256-680 1.82e-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: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  256 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 326
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  327 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 402
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  403 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 477
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  478 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 556
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  557 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 625
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652984  626 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 680
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1012-1087 4.47e-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: 4.47e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652984 1012 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1087
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 266-474 7.98e-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: 7.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  266 LKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 336
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  337 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 415
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652984  416 HVLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPHVV 474
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
TUDOR pfam00567
Tudor domain;
749-841 3.54e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.96  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  749 YETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKTLFQRVQVLEASQKedtwglGSVLVKFIDEGRTKLITRDQLLLLP 828
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD------GLVEVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 1958652984  829 EKFHTLPPQAVEF 841
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEXDc smart00487
DEAD-like helicases superfamily;
323-475 3.03e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 3.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984   323 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 396
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984   397 LTYRSLLFLRLCHLVLDEVHVLF-FEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNRHIEHLVREFMKDPHVVI 475
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHRLLdGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 285-439 4.59e-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: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  285 SWPPIARGCDVVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 353
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  354 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHVLF---FEanEQMFAIL 430
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1958652984  431 DNFKKNVEV 439
Cdd:pfam00270  143 RRLPKKRQI 151
PTZ00424 PTZ00424
helicase 45; Provisional
 378-605 2.34e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  378 KLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEvhvlffeANEQM-----FAILDNFKK---NVEVEE-RESAPHQ 448
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE-------ADEMLsrgfkGQIYDVFKKlppDVQVALfSATMPNE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  449 IVavgvhwnrhieHLVREFMKDPHVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFVP-SQAqktLIFTCSVAET 527
Cdd:PTZ00424   215 IL-----------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKV 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  528 EIVCKVVESNSIFCLKMHKEMAFNLKSILeqwKKKLSSGSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVFGG 603
Cdd:PTZ00424   281 DYLTKKMHERDFTVSCMHGDMDQKDRDLI---MREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIH 353


                   ..
gi 1958652984  604 RL 605
Cdd:PTZ00424   354 RI 355
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 733-855 8.20e-43

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: 152.40  E-value: 8.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  733 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKT-LFQRVQVLEASQKEDTW 801
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652984  802 GLGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 855
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
256-680 1.82e-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: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  256 TLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQmggcyKSLP 326
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTG-----------TgktaafllpLLQ-----RLDP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  327 SR-NGPLAVIVCPgwkkAQFI---FELLGDYSmssrPLHpVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSL 402
Cdd:COG0513     67 SRpRAPQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGAL 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  403 LFLRLCHLVLDEVhvlffeanEQMfaiLDN-FKKNVE-VEERESAPHQIV---AVgvhWNRHIEHLVREFMKDPhVVITA 477
Cdd:COG0513    142 DLSGVETLVLDEA--------DRM---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEV 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  478 LEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSIL 556
Cdd:COG0513    207 APENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQrERAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  557 EQWKkklsSGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKVF----G--GRlycmsdhfqslteqgspaeqG 625
Cdd:COG0513    285 DAFR----NGKIRVLVATD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR--------------------A 335

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652984  626 GKKTKSVLLLTERNASHavgvLRYLERAdAKIPSELYEFTAGVLEAKEDKKARRP 680
Cdd:COG0513    336 GAEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1012-1087 4.47e-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: 4.47e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652984 1012 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRACW 1087
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1008-1112 3.44e-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: 3.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984 1008 PQIKWFQKDDHIILKIKIRNVKDYKCKFFTDRVIFSAWVG--DKFYLADMELQGDIRKDDCKCIIKDDEPLITLAKEKRA 1085
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958652984 1086 -CWCGLLKQ--RNPNVAFDFDHWeeCEEDS 1112
Cdd:cd06465     81 eYWPRLTKEkgKLPWLKVDFDKW--VDEDE 108
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 266-474 7.98e-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: 7.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  266 LKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 336
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  337 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 415
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652984  416 HVLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPHVV 474
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 323-476 7.58e-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: 7.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  323 KSLPSRNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKNmKLPRGCDVIVTTPHSLLRLLTYRSL 402
Cdd:cd17952     56 RELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKAT 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958652984  403 LFLRLCHLVLDEVHVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDPhVVIT 476
Cdd:cd17952    134 NLQRVTYLVLDEADRMFdmgFEY--QVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDP-IRVV 197
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 330-475 1.25e-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: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  330 GPLAVIVCPGWKKAQFIFELLGDYSMSSrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCH 409
Cdd:cd17957     60 GLRALILAPTRELASQIYRELLKLSKGT-GLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEY 138

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652984  410 LVLDEVHVLF---F-EANEQMFAILDNFKKNVEVeerESA--PHQivavgvhwnrhIEHLVREFMKDPHVVI 475
Cdd:cd17957    139 LVLDEADKLFepgFrEQTDEILAACTNPNLQRSL---FSAtiPSE-----------VEELARSVMKDPIRII 196
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 248-470 1.92e-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: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  248 RNRIEPCLTLDKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPLLYLPPLLTI-------LQMGg 320
Cdd:cd18049     17 HNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVhinhqpfLERG- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  321 cykslpsrNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYR 400
Cdd:cd18049     96 --------DGPICLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAG 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652984  401 SLLFLRLCHLVLDEVHVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKD 470
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 ...
 329-476 2.88e-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: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  329 NGPLAVIVCPGWKKAQFI---FELLGDYsmssRPLhPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFL 405
Cdd:cd17945     65 DGPYALILAPTRELAQQIeeeTQKFAKP----LGI-RVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  406 RLCHLVLDEVHVLF---FEanEQMFAILDNFKKNVEVEERESAPHQiVAVGVHWNRH-----------IEHLVREFMKDP 471
Cdd:cd17945    140 QCTYVVLDEADRMIdmgFE--PQVTKILDAMPVSNKKPDTEEAEKL-AASGKHRYRQtmmftatmppaVEKIAKGYLRRP 216


                   ....*
gi 1958652984  472 hVVIT 476
Cdd:cd17945    217 -VVVT 220
TUDOR pfam00567
Tudor domain;
749-841 3.54e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.96  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  749 YETLNAEMNEYFKDPSNKTAAEKVENLGLYGLEEKTLFQRVQVLEASQKedtwglGSVLVKFIDEGRTKLITRDQLLLLP 828
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD------GLVEVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 1958652984  829 EKFHTLPPQAVEF 841
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEXDc smart00487
DEAD-like helicases superfamily;
323-475 3.03e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 3.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984   323 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 396
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984   397 LTYRSLLFLRLCHLVLDEVHVLF-FEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNRHIEHLVREFMKDPHVVI 475
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHRLLdGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 285-439 4.59e-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: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  285 SWPPIARGCDVVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 353
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  354 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHVLF---FEanEQMFAIL 430
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1958652984  431 DNFKKNVEV 439
Cdd:pfam00270  143 RRLPKKRQI 151
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 487-601 7.18e-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: 7.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  487 VQQVVHLCLECEKTSTLLQVLdFVPSQAQKTLIFTCSVAETEIVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKkklsS 565
Cdd:cd18787      1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEErERALKKFR----S 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958652984  566 GSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVF 601
Cdd:cd18787     76 GKVRVLVATD----VAArgldIPGVDHVINYDLPRDAEDY 111
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 268-471 1.22e-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: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  268 KALQRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPllylppllTILQMggcyksLPS------------RNGPLAVI 335
Cdd:cd17966      3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGK--------TLAFL------LPAivhinaqpplerGDGPIVLV 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  336 VCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKnMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV 415
Cdd:cd17966     69 LAPTRELAQQIQQEANKFGGSSR-LRNTCVYGGAPKGPQI-RDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEA 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652984  416 HVLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKDP 471
Cdd:cd17966    147 DRMLdmgFEP--QIRKIVDQIRPD----------RQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 323-434 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 1958652984  323 KSLP--SRNGPLAVIVCPGWKKAQFIFELLGDY----SMSSRPLHPVLLTIG--LHKDEAKNMKlpRGCDVIVTTPHSLL 394
Cdd:cd17951     57 KKLPfiKGEGPYGLIVCPSRELARQTHEVIEYYckalQEGGYPQLRCLLCIGgmSVKEQLEVIR--KGVHIVVATPGRLM 134

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958652984  395 RLLTYRsLLFLRLC-HLVLDEVHVLF---FEanEQMFAILDNFK 434
Cdd:cd17951    135 DMLNKK-KINLDICrYLCLDEADRMIdmgFE--EDIRTIFSYFK 175
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 266-471 1.79e-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: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  266 LKKAL-QRNKFPGPSHTASYSWPPIARGCDVVVISHCGNDPllylppllT------ILQMGGCYKSLPSRN-GPLAVIVC 337
Cdd:cd17949      1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGK--------TlayllpIIQRLLSLEPRVDRSdGTLALVLV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  338 PGWKKAQFIFELLGDYSMSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLL-RLLTYRSLLFLRLCHLVLDEVH 416
Cdd:cd17949     73 PTRELALQIYEVLEKLLKPFHWIVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEAD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652984  417 VLF---FEAN-EQMFAILDNFKKNVEVEERESAPHQIVAVGVHWNRHIEHLVREFMKDP 471
Cdd:cd17949    152 RLLdmgFEKDiTKILELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 322-453 2.18e-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: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  322 YKSLPSR--NGPLAVIVCPGWKKAQFIFELLGDYSmSSRPLHPVLLTIGLHKdeaKNMKLPR--GCDVIVTTPHSLLRLL 397
Cdd:cd17948     55 YKLLAEGpfNAPRGLVITPSRELAEQIGSVAQSLT-EGLGLKVKVITGGRTK---RQIRNPHfeEVDILVATPGALSKLL 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652984  398 TYR--SLLFLRlcHLVLDEVHVLFFEA-NEQMFAILDNF---KKNVEVEERESAPHQIVAVG 453
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 ...
 1007-1107 2.46e-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: 41.72  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984 1007 HPQIKWFQKDDHIILKIKIRNVKDYKCKFFTDRVIFSAWVGDKF-YLADMELQGDIRKDDCKCIIKDDEPLITLAK-EKR 1084
Cdd:cd00237      1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVkIYNEIELYDRVDPNDSKHKRTDRSILCCLRKgKEG 80

                           90       100
                   ....*....|....*....|....*
gi 1958652984 1085 ACWCGLLKQR-NPN-VAFDFDHWEE 1107
Cdd:cd00237     81 VAWPRLTKEKaKPNwLSVDFDNWRD 105
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 805-854 1.02e-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: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958652984  805 SVLVKFIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIE 854
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 ...
 197-470 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 1958652984  197 RLTEKK-DCDEKNGCVKLLQFLNPDPLRADEiSDLHQLQKVKLGTLQPGVVLRnriePCLTLDKSPLSADLKKALQRNKF 275
Cdd:cd18050      8 RLRKKKwDLSELPKFEKNFYVEHPEVARMTQ-YDVEELRRKKEITIRGVGCPK----PVFAFHQANFPQYVMDVLLDQNF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  276 PGPSHTASYSWPPIARGCDVVVISHCGNDPLLYLPPLLTILQMGGCYksLPSRNGPLAVIVCPGWKKAQFIFELLGDYSM 355
Cdd:cd18050     83 KEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY--LERGDGPICLVLAPTRELAQQVQQVADDYGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  356 SSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEVHVLF---FEAneQMFAILDN 432
Cdd:cd18050    161 SSR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLdmgFEP--QIRKIVDQ 236

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958652984  433 FKKNveveeresapHQIVAVGVHWNRHIEHLVREFMKD 470
Cdd:cd18050    237 IRPD----------RQTLMWSATWPKEVRQLAEDFLRD 264
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 1012-1081 1.86e-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: 38.34  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984 1012 WFQKDDHIILKIKIRNV--KDYKCKFFTDRVIFSA---------WVGDKFYLaDMELQGDIRKDDCKCIIKDDEPLITLA 1080
Cdd:cd00298      1 WYQTDDEVVVTVDLPGVkkEDIKVEVEDNVLTISGkreeeeereRSYGEFER-SFELPEDVDPEKSKASLENGVLEITLP 79


                   .
gi 1958652984 1081 K 1081
Cdd:cd00298     80 K 80
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 353-419 2.21e-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: 2.21e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652984  353 YSMSSRPLHPVLLTIGLHK--DEAKNMKL----PRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEVHVLF 419
Cdd:cd17965    126 YSVLKKLSHTVKLGIKTFSsgFGPSYQRLqlafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLF 198
PTZ00424 PTZ00424
helicase 45; Provisional
 378-605 2.34e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  378 KLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEvhvlffeANEQM-----FAILDNFKK---NVEVEE-RESAPHQ 448
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE-------ADEMLsrgfkGQIYDVFKKlppDVQVALfSATMPNE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  449 IVavgvhwnrhieHLVREFMKDPHVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFVP-SQAqktLIFTCSVAET 527
Cdd:PTZ00424   215 IL-----------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKV 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  528 EIVCKVVESNSIFCLKMHKEMAFNLKSILeqwKKKLSSGSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPKVFGG 603
Cdd:PTZ00424   281 DYLTKKMHERDFTVSCMHGDMDQKDRDLI---MREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIH 353


                   ..
gi 1958652984  604 RL 605
Cdd:PTZ00424   354 RI 355
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 750-838 3.11e-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: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  750 ETLNAEMNEYFKDPSNKTA--AEKVENLGLYGLEEKTLFqRVQVLEASQKEdtwglgsVLVKFIDEGRTKLITRDQLLLL 827
Cdd:cd20427      1 EQMEDEMKEFYSKSSTAMClrSPSVGQLVAVKAEEDAWL-RAQVIEVEEDK-------VKVYYVDHGFSEVVERSKLFKL 72

                           90
                   ....*....|.
gi 1958652984  828 PEKFHTLPPQA 838
Cdd:cd20427     73 NKQFYSLPFQA 83
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 729-835 3.32e-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: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  729 FYISNATNyfgriIDKHVDLYETLNAEMNEYFKDPSNK------TAAEKVENLGLYgleektlfqRVQVLEASqkedtwG 802
Cdd:cd20441      5 FFIQLSED-----EKVILQLAEELNETSEKSRENAAVKlkvgdlVAAEYDEDLALY---------RAVITAVL------P 64

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958652984  803 LGSVLVKFIDEGRTKLITRDQLLLLPEKFHTLP 835
Cdd:cd20441     65 GKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 322-414 6.50e-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: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652984  322 YKSLPSRNGPLAVIVCPGWKKAQFIFELLGDY-SMSSRPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYR 400
Cdd:cd17960     55 RKANLKKGQVGALIISPTRELATQIYEVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRK 134

                           90
                   ....*....|....*.
gi 1958652984  401 SLL--FLRLCHLVLDE 414
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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