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Conserved domains on  [gi|1720424213|ref|XP_030098859|]
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putative ATP-dependent RNA helicase TDRD12 isoform X2 [Mus musculus]

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 ...
 1-127 4.02e-72

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: 237.32  E-value: 4.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMCQDVE-MKPLMLEEGQVCVVYCQELKCWCRALIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQ 79
Cdd:cd20434     37 MNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMK 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720424213   80 LPYRAKKFRLYGTKPVTLHIDFCEDNAEIVPATKWDSAAIQYFQNLLR 127
Cdd:cd20434    117 LPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 825-947 8.52e-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: 149.71  E-value: 8.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  825 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKESSNKTSAEKVENLGLYGLEEKT-LFQRVQVLEVSQKEDTW 893
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720424213  894 GLGSILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 947
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
alpha-crystallin-Hsps_p23-like super family cl00175
alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a ...
 1100-1204 9.73e-12

alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.; The alpha-crystallin-Hsps_p23-like superfamily 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 superfamily 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).


The actual alignment was detected with superfamily member cd06465:

Pssm-ID: 469641 [Multi-domain]  Cd Length: 108  Bit Score: 62.61  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213 1100 PQIKWFQKDDVVILKIKIRNVKDYKCKFFTDRVIFSAWVG--DKFYLADLELQGDIRKDDCKCIIKDDEPLITLAKEKQ- 1176
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAg 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720424213 1177 ECWCGLLKQ--RNPNVAFDFDHWeeCEEDS 1204
Cdd:cd06465     81 EYWPRLTKEkgKLPWLKVDFDKW--VDEDE 108
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
469-772 1.17e-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: 68.25  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  469 MKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HML---FFEANEQMFAILDnfkknvevEERE----SA--P 538
Cdd:COG0513    116 RALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEAdRMLdmgFIEDIERILKLLP--------KERQtllfSAtmP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  539 HQivavgvhwnkhIDHLVREFMKDPcVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAE 618
Cdd:COG0513    188 PE-----------IRKLAKRYLKNP-VRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRG 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  619 TETVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKKklspGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKV 692
Cdd:COG0513    254 ADRLAEKLQKRGISAAALHGDLSQGQrERALDAFRN----GKIRVLVATD-----VAargidIDDVSHVINYDLPEDPED 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  693 L----G--GRlycmsdhfqslteqgspaeqGDKKTKSVLLLTERNASHAVGILRYLER--ADAKIPSELYEFTAGVLEAK 764
Cdd:COG0513    325 YvhriGrtGR--------------------AGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLK 384


                   ....*...
gi 1720424213  765 EDKKARRP 772
Cdd:COG0513    385 PKIKEKLK 392
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 358-563 4.97e-10

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member cd00268:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 196  Bit Score: 60.53  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  358 LKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 428
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  429 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 507
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424213  508 HMLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDP 563
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNP 192
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 1-127 4.02e-72

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: 237.32  E-value: 4.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMCQDVE-MKPLMLEEGQVCVVYCQELKCWCRALIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQ 79
Cdd:cd20434     37 MNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMK 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720424213   80 LPYRAKKFRLYGTKPVTLHIDFCEDNAEIVPATKWDSAAIQYFQNLLR 127
Cdd:cd20434    117 LPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 825-947 8.52e-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: 149.71  E-value: 8.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  825 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKESSNKTSAEKVENLGLYGLEEKT-LFQRVQVLEVSQKEDTW 893
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720424213  894 GLGSILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 947
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
TUDOR pfam00567
Tudor domain;
1-91 3.24e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 75.85  E-value: 3.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMCQdvEMKPLMLEEGQVCVVYCQElkCWCRALIKSIIssaDHYLAECFLVDFAKYIPVKSKNIRVAVESFMQL 80
Cdd:pfam00567   34 LQEYYASKPP--ESLPPAVGDGCVAAFSEDG--KWYRAKITESL---DDGLVEVLFIDYGNTETVPLSDLRPLPPELESL 106

                           90
                   ....*....|.
gi 1720424213   81 PYRAKKFRLYG 91
Cdd:pfam00567  107 PPQAIKCQLAG 117
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1100-1204 9.73e-12

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: 62.61  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213 1100 PQIKWFQKDDVVILKIKIRNVKDYKCKFFTDRVIFSAWVG--DKFYLADLELQGDIRKDDCKCIIKDDEPLITLAKEKQ- 1176
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAg 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720424213 1177 ECWCGLLKQ--RNPNVAFDFDHWeeCEEDS 1204
Cdd:cd06465     81 EYWPRLTKEkgKLPWLKVDFDKW--VDEDE 108
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
469-772 1.17e-11

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 68.25  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  469 MKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HML---FFEANEQMFAILDnfkknvevEERE----SA--P 538
Cdd:COG0513    116 RALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEAdRMLdmgFIEDIERILKLLP--------KERQtllfSAtmP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  539 HQivavgvhwnkhIDHLVREFMKDPcVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAE 618
Cdd:COG0513    188 PE-----------IRKLAKRYLKNP-VRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRG 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  619 TETVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKKklspGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKV 692
Cdd:COG0513    254 ADRLAEKLQKRGISAAALHGDLSQGQrERALDAFRN----GKIRVLVATD-----VAargidIDDVSHVINYDLPEDPED 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  693 L----G--GRlycmsdhfqslteqgspaeqGDKKTKSVLLLTERNASHAVGILRYLER--ADAKIPSELYEFTAGVLEAK 764
Cdd:COG0513    325 YvhriGrtGR--------------------AGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLK 384


                   ....*...
gi 1720424213  765 EDKKARRP 772
Cdd:COG0513    385 PKIKEKLK 392
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 358-563 4.97e-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: 60.53  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  358 LKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 428
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  429 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 507
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424213  508 HMLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDP 563
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNP 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 415-566 9.96e-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: 9.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  415 KSLPSRNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKNmKLPRGCDVIVTTPHSLLRLLTYRSL 494
Cdd:cd17952     56 RELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKAT 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720424213  495 LFLRLCHLVLDEVHMLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDPCVV 566
Cdd:cd17952    134 NLQRVTYLVLDEADRMFdmgFEY--QVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDPIRV 196
TUDOR pfam00567
Tudor domain;
815-933 1.01e-05

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 45.81  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  815 HIRVIPFYISNATNYFGRIIDKHVDLyETLNAEMNEYFKESSNKTSAEKVENLGLYGLEEKTLFQRVQVLEVSQKedtwg 894
Cdd:pfam00567    2 TIDVVVSHIESPSTFYIQPKSDSKKL-EKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD----- 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720424213  895 lGSILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEF 933
Cdd:pfam00567   76 -GLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKC 113
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 377-531 3.42e-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: 45.70  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  377 SWPPIARGCDMVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 445
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  446 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHMLF---FEanEQMFAIL 522
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1720424213  523 DNFKKNVEV 531
Cdd:pfam00270  143 RRLPKKRQI 151
DEXDc smart00487
DEAD-like helicases superfamily;
415-567 4.69e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 45.95  E-value: 4.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213   415 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 488
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213   489 LTYRSLLFLRLCHLVLDEVH-MLFFEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNKHIDHLVREFMKDPCVVI 567
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
PTZ00110 PTZ00110
helicase; Provisional
 319-753 4.94e-05

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 47.46  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  319 TSDLHQLQKVKLGTLQPGvvlRNRIEPCLTLEKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGNDPL 398
Cdd:PTZ00110   105 SKEVDEIRKEKEITIIAG---ENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKT 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  399 LYLPPLLTI-------LQMGgcykslpsrNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKdEAKNMKL 471
Cdd:PTZ00110   182 LAFLLPAIVhinaqplLRYG---------DGPIVLVLAPTRELAEQIREQCNKFGASSK-IRNTVAYGGVPK-RGQIYAL 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  472 PRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HMLFFEANEQMFAILDNFKKNveveeresapHQIVAVGVHWNK 550
Cdd:PTZ00110   251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAdRMLDMGFEPQIRKIVSQIRPD----------RQTLMWSATWPK 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  551 HIDHLVREFMKDPCVVIT--ALEEAALYgSVQQVVHLCLECEKTSTLLQVLDFVPSQAQKTLIFTCSVAETETVCKVVES 628
Cdd:PTZ00110   321 EVQSLARDLCKEEPVHVNvgSLDLTACH-NIKQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRL 399

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  629 NSIFCLKMHKEMAFNLKS-ILEQWKKklspGSHIVLTLTDDCIPLLAITDATCVVHFSFPSSpkvlggrlycMSDHFQSL 707
Cdd:PTZ00110   400 DGWPALCIHGDKKQEERTwVLNEFKT----GKSPIMIATDVASRGLDVKDVKYVINFDFPNQ----------IEDYVHRI 465

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1720424213  708 TEQGSPAEQGdkktKSVLLLTE---RNASHAVGILRyleRADAKIPSEL 753
Cdd:PTZ00110   466 GRTGRAGAKG----ASYTFLTPdkyRLARDLVKVLR---EAKQPVPPEL 507
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 1-127 4.02e-72

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: 237.32  E-value: 4.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMCQDVE-MKPLMLEEGQVCVVYCQELKCWCRALIKSIISSADHYLAECFLVDFAKYIPVKSKNIRVAVESFMQ 79
Cdd:cd20434     37 MNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESLMSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMK 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720424213   80 LPYRAKKFRLYGTKPVTLHIDFCEDNAEIVPATKWDSAAIQYFQNLLR 127
Cdd:cd20434    117 LPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQNLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 825-947 8.52e-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: 149.71  E-value: 8.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  825 NATNYFGRIIDKH----------VDLYETLNAEMNEYFKESSNKTSAEKVENLGLYGLEEKT-LFQRVQVLEVSQKEDTW 893
Cdd:cd20435      1 DATHYSARILEHRssdgevtksmSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720424213  894 GLGSILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIEW 947
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
TUDOR pfam00567
Tudor domain;
1-91 3.24e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 75.85  E-value: 3.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMCQdvEMKPLMLEEGQVCVVYCQElkCWCRALIKSIIssaDHYLAECFLVDFAKYIPVKSKNIRVAVESFMQL 80
Cdd:pfam00567   34 LQEYYASKPP--ESLPPAVGDGCVAAFSEDG--KWYRAKITESL---DDGLVEVLFIDYGNTETVPLSDLRPLPPELESL 106

                           90
                   ....*....|.
gi 1720424213   81 PYRAKKFRLYG 91
Cdd:pfam00567  107 PPQAIKCQLAG 117
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1100-1204 9.73e-12

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: 62.61  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213 1100 PQIKWFQKDDVVILKIKIRNVKDYKCKFFTDRVIFSAWVG--DKFYLADLELQGDIRKDDCKCIIKDDEPLITLAKEKQ- 1176
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEAg 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720424213 1177 ECWCGLLKQ--RNPNVAFDFDHWeeCEEDS 1204
Cdd:cd06465     81 EYWPRLTKEkgKLPWLKVDFDKW--VDEDE 108
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
469-772 1.17e-11

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 68.25  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  469 MKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HML---FFEANEQMFAILDnfkknvevEERE----SA--P 538
Cdd:COG0513    116 RALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEAdRMLdmgFIEDIERILKLLP--------KERQtllfSAtmP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  539 HQivavgvhwnkhIDHLVREFMKDPcVVITALEEAALYGSVQQVVHLCLECEKTSTLLQVLDFvpSQAQKTLIFTCSVAE 618
Cdd:COG0513    188 PE-----------IRKLAKRYLKNP-VRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD--EDPERAIVFCNTKRG 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  619 TETVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKKklspGSHIVLTLTDdciplLA-----ITDATCVVHFSFPSSPKV 692
Cdd:COG0513    254 ADRLAEKLQKRGISAAALHGDLSQGQrERALDAFRN----GKIRVLVATD-----VAargidIDDVSHVINYDLPEDPED 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  693 L----G--GRlycmsdhfqslteqgspaeqGDKKTKSVLLLTERNASHAVGILRYLER--ADAKIPSELYEFTAGVLEAK 764
Cdd:COG0513    325 YvhriGrtGR--------------------AGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLK 384


                   ....*...
gi 1720424213  765 EDKKARRP 772
Cdd:COG0513    385 PKIKEKLK 392
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1104-1179 2.40e-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: 60.76  E-value: 2.40e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424213 1104 WFQKDDVVILKIKIRNV--KDYKCKFFTDRVIFSA-WVGDKFYLADLELQGDIRKDDCKCIIKDDEPLITLAKEKQECW 1179
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 358-563 4.97e-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: 60.53  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  358 LKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGndpllylppllT---------ILQMGgCYKSLPSRNGPLAVIV 428
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTG-----------SgktlafllpILEKL-LPEPKKKGRGPQALVL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  429 CPGWKKAQFIFELLGDYSmSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTyRSLLFLRLC-HLVLDEV 507
Cdd:cd00268     69 APTRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEA 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424213  508 HMLF---FEanEQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDP 563
Cdd:cd00268    146 DRMLdmgFE--EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNP 192
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 340-562 3.87e-08

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: 55.40  E-value: 3.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  340 RNRIEPCLTLEKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGNDPLLYLPPLLTI-------LQMGg 412
Cdd:cd18049     17 HNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVhinhqpfLERG- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  413 cykslpsrNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYR 492
Cdd:cd18049     96 --------DGPICLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAG 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424213  493 SLLFLRLCHLVLDEV-HMLFFEANEQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKD 562
Cdd:cd18049    166 KTNLRRCTYLVLDEAdRMLDMGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRQLAEDFLKD 226
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 21-71 5.24e-08

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: 50.21  E-value: 5.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720424213   21 EGQVCVVYCQELKCWCRALIKSIISSadhYLAECFLVDFAKYIPVKSKNIR 71
Cdd:cd20379      1 VGDLCAAKYEEDGKWYRARVLEVLSN---DKVEVFFVDYGNTETVPLSDLR 48
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 24-96 7.19e-07

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


Pssm-ID: 410494  Cd Length: 80  Bit Score: 48.25  E-value: 7.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720424213   24 VCVVYCQELKCWCRALIKSIISSADHylAECFLVDFAKYIPVKSKNIRVAVESFMQLPYRAKKFRLYGTKPVT 96
Cdd:cd20423      8 VCLAKYSEDGKWCRALIDNVYEPVEM--VEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPS 78
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 415-566 9.96e-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: 9.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  415 KSLPSRNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKNmKLPRGCDVIVTTPHSLLRLLTYRSL 494
Cdd:cd17952     56 RELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKAT 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720424213  495 LFLRLCHLVLDEVHMLF---FEAneQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDPCVV 566
Cdd:cd17952    134 NLQRVTYLVLDEADRMFdmgFEY--QVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 421-537 1.66e-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: 50.40  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  421 NGPLAVIVCPGWKKAQFI---FELLGDYsmssRPLhPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFL 497
Cdd:cd17945     65 DGPYALILAPTRELAQQIeeeTQKFAKP----LGI-RVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLN 139

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720424213  498 RLCHLVLDEVHMLF---FEanEQMFAILDNFKKNVEVEERESA 537
Cdd:cd17945    140 QCTYVVLDEADRMIdmgFE--PQVTKILDAMPVSNKKPDTEEA 180
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 422-522 8.33e-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: 47.97  E-value: 8.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  422 GPLAVIVCPGWKKAQFIFELLGDYSMSSrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCH 501
Cdd:cd17957     60 GLRALILAPTRELASQIYRELLKLSKGT-GLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEY 138

                           90       100
                   ....*....|....*....|...
gi 1720424213  502 LVLDEVHMLfFEAN--EQMFAIL 522
Cdd:cd17957    139 LVLDEADKL-FEPGfrEQTDEIL 160
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 360-563 9.88e-06

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: 47.75  E-value: 9.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  360 KALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGNDpllylpplLTILQMggcyksLPS------------RNGPLAVI 427
Cdd:cd17966      3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSG--------KTLAFL------LPAivhinaqpplerGDGPIVLV 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  428 VCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKDEAKnMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV 507
Cdd:cd17966     69 LAPTRELAQQIQQEANKFGGSSR-LRNTCVYGGAPKGPQI-RDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEA 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720424213  508 -HMLFFEANEQMFAILDNFKKNveveeresapHQIVAVGVHWNKHIDHLVREFMKDP 563
Cdd:cd17966    147 dRMLDMGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRRLAEDFLKDY 193
TUDOR pfam00567
Tudor domain;
815-933 1.01e-05

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 45.81  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  815 HIRVIPFYISNATNYFGRIIDKHVDLyETLNAEMNEYFKESSNKTSAEKVENLGLYGLEEKTLFQRVQVLEVSQKedtwg 894
Cdd:pfam00567    2 TIDVVVSHIESPSTFYIQPKSDSKKL-EKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDD----- 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720424213  895 lGSILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEF 933
Cdd:pfam00567   76 -GLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKC 113
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 377-531 3.42e-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: 45.70  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  377 SWPPIARGCDMVVISHCGndpllylpplltilqmGGcyKSL-----------PSRNGPLAVIVCPGWKKAQFIFELLGDY 445
Cdd:pfam00270    7 AIPAILEGRDVLVQAPTG----------------SG--KTLafllpalealdKLDNGPQALVLAPTRELAEQIYEELKKL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  446 SmsSRPLHPVLLTIGLHKDEAKNMKLpRGCDVIVTTPHSLLRLLTYRSLLFlRLCHLVLDEVHMLF---FEanEQMFAIL 522
Cdd:pfam00270   69 G--KGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLdmgFG--PDLEEIL 142


                   ....*....
gi 1720424213  523 DNFKKNVEV 531
Cdd:pfam00270  143 RRLPKKRQI 151
DEXDc smart00487
DEAD-like helicases superfamily;
415-567 4.69e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 45.95  E-value: 4.69e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213   415 KSLPSRNGPLAVIVCP------GWKKAqfiFELLGDYSmssrPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRL 488
Cdd:smart00487   47 EALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDL 119

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213   489 LTYRSLLFLRLCHLVLDEVH-MLFFEANEQMFAILDNFKKNVeveeresaphQIVAVGVHWNKHIDHLVREFMKDPCVVI 567
Cdd:smart00487  120 LENDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPVFID 189
PTZ00110 PTZ00110
helicase; Provisional
 319-753 4.94e-05

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 47.46  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  319 TSDLHQLQKVKLGTLQPGvvlRNRIEPCLTLEKSPLSADLKKALQRNKFPGPSHTASYSWPPIARGCDMVVISHCGNDPL 398
Cdd:PTZ00110   105 SKEVDEIRKEKEITIIAG---ENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKT 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  399 LYLPPLLTI-------LQMGgcykslpsrNGPLAVIVCPGWKKAQFIFELLGDYSMSSRpLHPVLLTIGLHKdEAKNMKL 471
Cdd:PTZ00110   182 LAFLLPAIVhinaqplLRYG---------DGPIVLVLAPTRELAEQIREQCNKFGASSK-IRNTVAYGGVPK-RGQIYAL 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  472 PRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HMLFFEANEQMFAILDNFKKNveveeresapHQIVAVGVHWNK 550
Cdd:PTZ00110   251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAdRMLDMGFEPQIRKIVSQIRPD----------RQTLMWSATWPK 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  551 HIDHLVREFMKDPCVVIT--ALEEAALYgSVQQVVHLCLECEKTSTLLQVLDFVPSQAQKTLIFTCSVAETETVCKVVES 628
Cdd:PTZ00110   321 EVQSLARDLCKEEPVHVNvgSLDLTACH-NIKQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRL 399

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  629 NSIFCLKMHKEMAFNLKS-ILEQWKKklspGSHIVLTLTDDCIPLLAITDATCVVHFSFPSSpkvlggrlycMSDHFQSL 707
Cdd:PTZ00110   400 DGWPALCIHGDKKQEERTwVLNEFKT----GKSPIMIATDVASRGLDVKDVKYVINFDFPNQ----------IEDYVHRI 465

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1720424213  708 TEQGSPAEQGdkktKSVLLLTE---RNASHAVGILRyleRADAKIPSEL 753
Cdd:PTZ00110   466 GRTGRAGAKG----ASYTFLTPdkyRLARDLVKVLR---EAKQPVPPEL 507
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 579-691 5.84e-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: 44.04  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  579 VQQVVHLCLECEKTSTLLQVLdFVPSQAQKTLIFTCSVAETETVCKVVESNSIFCLKMHKEMAFNL-KSILEQWKKklsp 657
Cdd:cd18787      1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEErERALKKFRS---- 75

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720424213  658 GSHIVLTLTDdcipLLA----ITDATCVVHFSFPSSPK 691
Cdd:cd18787     76 GKVRVLVATD----VAArgldIPGVDHVINYDLPRDAE 109
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 289-562 6.48e-05

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: 46.16  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  289 RLTEKK-DCDEKNGCVKllQFLNPDPLRADGTS-DLHQLQKVKLGTLQPGVVLRnriePCLTLEKSPLSADLKKALQRNK 366
Cdd:cd18050      8 RLRKKKwDLSELPKFEK--NFYVEHPEVARMTQyDVEELRRKKEITIRGVGCPK----PVFAFHQANFPQYVMDVLLDQN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  367 FPGPSHTASYSWPPIARGCDMVVISHCGNDPLLYLPPLLTILQMGGCYksLPSRNGPLAVIVCPGWKKAQFIFELLGDYS 446
Cdd:cd18050     82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY--LERGDGPICLVLAPTRELAQQVQQVADDYG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  447 MSSRpLHPVLLTIGLHKDeAKNMKLPRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEV-HMLFFEANEQMFAILDNF 525
Cdd:cd18050    160 KSSR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAdRMLDMGFEPQIRKIVDQI 237

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1720424213  526 KKNveveeresapHQIVAVGVHWNKHIDHLVREFMKD 562
Cdd:cd18050    238 RPD----------RQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 415-526 7.03e-05

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: 45.41  E-value: 7.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  415 KSLP--SRNGPLAVIVCPGWKKAQFIFELLGDY----SMSSRPLHPVLLTIG--LHKDEAKNMKlpRGCDVIVTTPHSLL 486
Cdd:cd17951     57 KKLPfiKGEGPYGLIVCPSRELARQTHEVIEYYckalQEGGYPQLRCLLCIGgmSVKEQLEVIR--KGVHIVVATPGRLM 134

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720424213  487 RLLTYRsLLFLRLC-HLVLDE----VHMLFfeaNEQMFAILDNFK 526
Cdd:cd17951    135 DMLNKK-KINLDICrYLCLDEadrmIDMGF---EEDIRTIFSYFK 175
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 358-563 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  358 LKKAL-QRNKFPGPSHTASYSWPPIARGCDMVVISHCGNDPllylppllT------ILQMGGCYKSLPSRN-GPLAVIVC 429
Cdd:cd17949      1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGK--------TlayllpIIQRLLSLEPRVDRSdGTLALVLV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  430 PGWKKAQFIFELLGDYSMSSRPLHPVLLtIGLHKDEAKNMKLPRGCDVIVTTPHSLL-RLLTYRSLLFLRLCHLVLDE-- 506
Cdd:cd17949     73 PTRELALQIYEVLEKLLKPFHWIVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEad 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424213  507 --VHMLFFEANEQMFAILDNFKKNVEVEERESAPHQIVAVGVHWNKHIDHLVREFMKDP 563
Cdd:cd17949    152 rlLDMGFEKDITKILELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 1099-1199 2.37e-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: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213 1099 HPQIKWFQKDDVVILKIKIRNVKDYKCKFFTDRVIFSAWVGDKF-YLADLELQGDIRKDDCKCIIKDDEPLITLAK-EKQ 1176
Cdd:cd00237      1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVkIYNEIELYDRVDPNDSKHKRTDRSILCCLRKgKEG 80

                           90       100
                   ....*....|....*....|....*
gi 1720424213 1177 ECWCGLLKQR-NPN-VAFDFDHWEE 1199
Cdd:cd00237     81 VAWPRLTKEKaKPNwLSVDFDNWRD 105
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 414-545 2.93e-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: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  414 YKSLPSR--NGPLAVIVCPGWKKAQFIFELLGDYSmSSRPLHPVLLTIGLHKdeaKNMKLPR--GCDVIVTTPHSLLRLL 489
Cdd:cd17948     55 YKLLAEGpfNAPRGLVITPSRELAEQIGSVAQSLT-EGLGLKVKVITGGRTK---RQIRNPHfeEVDILVATPGALSKLL 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720424213  490 TYR--SLLFLRlcHLVLDEVHMLFFEA-NEQMFAILDNF---KKNVEVEERESAPHQIVAVG 545
Cdd:cd17948    131 TSRiySLEQLR--HLVLDEADTLLDDSfNEKLSHFLRRFplaSRRSENTDGLDPGTQLVLVS 190
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 842-930 1.82e-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: 38.95  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  842 ETLNAEMNEYFKESSNKTS--AEKVENLGLYGLEEKTLFqRVQVLEVSQKEdtwglgsILVKLIDEGRTKLITRDQLLLL 919
Cdd:cd20427      1 EQMEDEMKEFYSKSSTAMClrSPSVGQLVAVKAEEDAWL-RAQVIEVEEDK-------VKVYYVDHGFSEVVERSKLFKL 72

                           90
                   ....*....|.
gi 1720424213  920 PEKFHTLPPQA 930
Cdd:cd20427     73 NKQFYSLPFQA 83
Tudor_TDRD7_rpt3 cd20429
third Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 1-84 2.13e-03

third 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 third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410500  Cd Length: 91  Bit Score: 38.62  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213    1 MNDFYNSMcqdvEMKPLMLEEGQVCVVYCQELkcWCRALIKSIISSAdhyLAECFLVDFAKYIPVKSKNIRVAVESFMQL 80
Cdd:cd20429     16 MILYYNKT----EERPVAIEKNKVYAAKIENN--WYRVLVKGILTNG---LVSVYELDYGKHELVSIRKVQPLIEKFRQL 86


                   ....
gi 1720424213   81 PYRA 84
Cdd:cd20429     87 PFQA 90
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 445-511 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720424213  445 YSMSSRPLHPVLLTIGLHK--DEAKNMKL----PRGCDVIVTTPHSLLRLLTYRSLLFLRLCHLVLDEVHMLF 511
Cdd:cd17965    126 YSVLKKLSHTVKLGIKTFSsgFGPSYQRLqlafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLF 198
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 414-506 6.39e-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: 39.48  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424213  414 YKSLPSRNGPLAVIVCPGWKKAQFIFELLGDY-SMSSRPLHPVLLTIGLHKDEAKNMKLPRGCDVIVTTPHSLLRLLTYR 492
Cdd:cd17960     55 RKANLKKGQVGALIISPTRELATQIYEVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRK 134

                           90
                   ....*....|....*.
gi 1720424213  493 SLL--FLRLCHLVLDE 506
Cdd:cd17960    135 ADKvkVKSLEVLVLDE 150
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 897-946 7.77e-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: 37.39  E-value: 7.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720424213  897 SILVKLIDEGRTKLITRDQLLLLPEKFHTLPPQAVEFIVCRVKPADSEIE 946
Cdd:cd20418     34 KILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDSE 83
 
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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