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Conserved domains on  [gi|768011969|ref|XP_011525776|]
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putative ATP-dependent RNA helicase TDRD12 isoform X4 [Homo sapiens]

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 ...
 4-125 7.37e-59

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: 199.57  E-value: 7.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434     1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   82 TSSADQYLAECFLVDFAKNIPVKSKK----------------------------------------PAKKWDNAAIQYFQ 121
Cdd:cd20434    81 MSSADDYLAECFLVDYAKYIPVKSKDirvaleafmklpyrakkfrlygikpvtlhvdlcedkakivPARKWDSAAIQYFQ 160


                  ....
gi 768011969  122 NLLK 125
Cdd:cd20434   161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 857-978 1.10e-44

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: 157.80  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  857 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 924
Cdd:cd20435     1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  925 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 978
Cdd:cd20435    81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-799 3.99e-14

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: 75.95  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  377 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 450
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  451 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 527
Cdd:COG0513    71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  528 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 601
Cdd:COG0513   138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  602 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 677
Cdd:COG0513   210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  678 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 745
Cdd:COG0513   285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  746 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 799
Cdd:COG0513   337 AEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
alpha-crystallin-Hsps_p23-like super family cl00175
alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a ...
 1153-1257 4.56e-10

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: 57.99  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969 1153 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1229
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 768011969 1230 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1257
Cdd:cd06465    81 EYWPRLTKEkgKLPWLKVDFDKWVD--EDE 108
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 4-125 7.37e-59

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: 199.57  E-value: 7.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434     1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   82 TSSADQYLAECFLVDFAKNIPVKSKK----------------------------------------PAKKWDNAAIQYFQ 121
Cdd:cd20434    81 MSSADDYLAECFLVDYAKYIPVKSKDirvaleafmklpyrakkfrlygikpvtlhvdlcedkakivPARKWDSAAIQYFQ 160


                  ....
gi 768011969  122 NLLK 125
Cdd:cd20434   161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 857-978 1.10e-44

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: 157.80  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  857 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 924
Cdd:cd20435     1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  925 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 978
Cdd:cd20435    81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-799 3.99e-14

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 75.95  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  377 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 450
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  451 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 527
Cdd:COG0513    71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  528 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 601
Cdd:COG0513   138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  602 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 677
Cdd:COG0513   210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  678 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 745
Cdd:COG0513   285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  746 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 799
Cdd:COG0513   337 AEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 387-595 1.81e-13

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: 70.55  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVIS-------HCesnpllYLLPVLTVLQTgacyKSLPSRNGPLAVIVCP 459
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAqtgsgktLA------FLLPILEKLLP----EPKKKGRGPQALVLAP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  460 GWKKAQFIFELLGEYSmSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVEV 538
Cdd:cd00268    71 TRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEADR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768011969  539 L----FLeanEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 595
Cdd:cd00268   148 MldmgFE---EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
TUDOR pfam00567
Tudor domain;
10-107 7.41e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 63.53  E-value: 7.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    10 EDPGCFWVIIKGCSPF----LDHDVDYQKLNSAMNDFYNstCQDIEIKPLTLEEGQVCVVYCEElkCWCRAIvksITSSA 85
Cdd:pfam00567    1 STIDVVVSHIESPSTFyiqpKSDSKKLEKLTEELQEYYA--SKPPESLPPAVGDGCVAAFSEDG--KWYRAK---ITESL 73

                           90       100
                   ....*....|....*....|..
gi 768011969    86 DQYLAECFLVDFAKNIPVKSKK 107
Cdd:pfam00567   74 DDGLVEVLFIDYGNTETVPLSD 95
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1153-1257 4.56e-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: 57.99  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969 1153 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1229
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 768011969 1230 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1257
Cdd:cd06465    81 EYWPRLTKEkgKLPWLKVDFDKWVD--EDE 108
TUDOR pfam00567
Tudor domain;
873-964 3.76e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 47.35  E-value: 3.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   873 YATLNAEMNEYFKDSNKTTVE-KVEKFGLYGLAEKTLFHRVQVLEVNQKEDAwalddiLVEFIDEGRTGLVTRDQLLHLP 951
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEDGKWYRAKITESLDDGLV------EVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 768011969   952 EHFHTLPPQAVEF 964
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 406-560 2.05e-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: 46.08  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   406 SWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQtgacykslPSRNGPLAVIVCPGWKKAQFIFELLGEYSmsSR 479
Cdd:pfam00270    7 AIPAILEGRDVLVQA-----PtgsgktLAFLLPALEALD--------KLDNGPQALVLAPTRELAEQIYEELKKLG--KG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   480 PLHPVLLTIGLHKEEAKNTKLpRGCDVIVTTPYSLLRLLAcQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNI 558
Cdd:pfam00270   72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAhRLLDMGFGPDLEEILRRLPKKR 149


                   ..
gi 768011969   559 EV 560
Cdd:pfam00270  150 QI 151
DEXDc smart00487
DEAD-like helicases superfamily;
441-596 1.01e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 44.79  E-value: 1.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    441 ACYKSLPSRNGPLAVIVCP------GWKKAqfiFELLGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSL 514
Cdd:smart00487   44 PALEALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRL 116

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    515 LRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIeveeresaphQIVAVGVHWNKHIEHLIKEFMNDPY 593
Cdd:smart00487  117 LDLLENDKLSLSNVDLVILDEAhRLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPV 186


                    ...
gi 768011969    594 IVI 596
Cdd:smart00487  187 FID 189
PTZ00424 PTZ00424
helicase 45; Provisional
 499-783 2.71e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  499 KLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIEVEE-RESAPHQIVavgvh 576
Cdd:PTZ00424  142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAdEMLSRGFKGQIYDVFKKLPPDVQVALfSATMPNEIL----- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  577 wnkhieHLIKEFMNDPYIVITAMEEAALYGNVQQVVHLCLECEKTSSLLQALDFIP-SQAqktLIFTCSVAETEIVCKVV 655
Cdd:PTZ00424  217 ------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKVDYLTKKM 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  656 ESSSIFCLKMHKEMIfnlQNVLEQWKKKLSSGSQIILALTDdcvpLLA----ITDATCVIHFSFPASPKVFGGRLycmsd 731
Cdd:PTZ00424  288 HERDFTVSCMHGDMD---QKDRDLIMREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIHRI----- 355

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768011969  732 hfhaeqGSPAEQGdKKAKSVLLLTEKDASHAVGVLRYLERADAKVPAELYEF 783
Cdd:PTZ00424  356 ------GRSGRFG-RKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
 
Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 4-125 7.37e-59

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: 199.57  E-value: 7.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434     1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   82 TSSADQYLAECFLVDFAKNIPVKSKK----------------------------------------PAKKWDNAAIQYFQ 121
Cdd:cd20434    81 MSSADDYLAECFLVDYAKYIPVKSKDirvaleafmklpyrakkfrlygikpvtlhvdlcedkakivPARKWDSAAIQYFQ 160


                  ....
gi 768011969  122 NLLK 125
Cdd:cd20434   161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 857-978 1.10e-44

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: 157.80  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  857 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 924
Cdd:cd20435     1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  925 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 978
Cdd:cd20435    81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
377-799 3.99e-14

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 75.95  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  377 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 450
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  451 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 527
Cdd:COG0513    71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  528 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 601
Cdd:COG0513   138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  602 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 677
Cdd:COG0513   210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  678 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 745
Cdd:COG0513   285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011969  746 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 799
Cdd:COG0513   337 AEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 387-595 1.81e-13

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: 70.55  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVIS-------HCesnpllYLLPVLTVLQTgacyKSLPSRNGPLAVIVCP 459
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAqtgsgktLA------FLLPILEKLLP----EPKKKGRGPQALVLAP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  460 GWKKAQFIFELLGEYSmSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVEV 538
Cdd:cd00268    71 TRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEADR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768011969  539 L----FLeanEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 595
Cdd:cd00268   148 MldmgFE---EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
TUDOR pfam00567
Tudor domain;
10-107 7.41e-12

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 63.53  E-value: 7.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    10 EDPGCFWVIIKGCSPF----LDHDVDYQKLNSAMNDFYNstCQDIEIKPLTLEEGQVCVVYCEElkCWCRAIvksITSSA 85
Cdd:pfam00567    1 STIDVVVSHIESPSTFyiqpKSDSKKLEKLTEELQEYYA--SKPPESLPPAVGDGCVAAFSEDG--KWYRAK---ITESL 73

                           90       100
                   ....*....|....*....|..
gi 768011969    86 DQYLAECFLVDFAKNIPVKSKK 107
Cdd:pfam00567   74 DDGLVEVLFIDYGNTETVPLSD 95
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 369-596 1.79e-11

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: 65.42  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  369 RNKIKPCLTIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLT------VLQTGa 441
Cdd:cd18049    17 HNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLsYLLPAIVhinhqpFLERG- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  442 cykslpsrNGPLAVIVCPGWKKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEeAKNTKLPRGCDVIVTTPYSLLRLLACQ 521
Cdd:cd18049    96 --------DGPICLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAG 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768011969  522 SLLFLRLCHLILDEVE-VLFLEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDpYIVI 596
Cdd:cd18049   166 KTNLRRCTYLVLDEADrMLDMGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRQLAEDFLKD-YIHI 230
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1153-1257 4.56e-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: 57.99  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969 1153 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1229
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 768011969 1230 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1257
Cdd:cd06465    81 EYWPRLTKEkgKLPWLKVDFDKWVD--EDE 108
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 387-595 8.16e-10

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: 60.29  E-value: 8.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKAL-QRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQtgaCYKSLPSRN-GPLAVIVCPGWKK 463
Cdd:cd17949     1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLaYLLPIIQRLL---SLEPRVDRSdGTLALVLVPTREL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  464 AQFIFELLGEYSMSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLL-RLLACQSLLFLRLCHLILDEVEVL--- 539
Cdd:cd17949    78 ALQIYEVLEKLLKPFHWIVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLldm 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768011969  540 -FLEANEQMFAILDNFKKNIEVEERESAPHQIVAVGVHWNKHIEHLIKEFMNDP-YIV 595
Cdd:cd17949   157 gFEKDITKILELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPvYID 214
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 389-595 6.22e-09

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: 57.38  E-value: 6.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  389 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLT------VLQTGacykslpsrNGPLAVIVCPGW 461
Cdd:cd17966     3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLaFLLPAIVhinaqpPLERG---------DGPIVLVLAPTR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  462 KKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVE-VLF 540
Cdd:cd17966    74 ELAQQIQQEANKFGGSSR-LRNTCVYGGAPKGPQIR-DLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADrMLD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768011969  541 LEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 595
Cdd:cd17966   152 MGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 429-553 9.12e-08

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: 53.75  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  429 YLLPVLTVLQTgacyksLPSRNGPLAVIVCPGWKKAQFIFELLGEYSMSSrPLHPVLLTIGLHKEEAKNTKLPRGCDVIV 508
Cdd:cd17957    44 FLIPILQKLGK------PRKKKGLRALILAPTRELASQIYRELLKLSKGT-GLRIVLLSKSLEAKAKDGPKSITKYDILV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 768011969  509 TTPYSLLRLLaCQSLLFLR-LCHLILDEVEVL----FLEANEQMFAILDN 553
Cdd:cd17957   117 STPLRLVFLL-KQGPIDLSsVEYLVLDEADKLfepgFREQTDEILAACTN 165
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1157-1236 1.38e-07

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: 50.36  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969 1157 WFQKEDVVILKIRIRNV--KDYKCQYLRDRVVFSA-WVGDKFYLADLELRGNIRKDDCQCVIRNDEPVITLAKE-RREAW 1232
Cdd:cd06463     1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKePGEWW 80


                  ....
gi 768011969 1233 CHLL 1236
Cdd:cd06463    81 PRLE 84
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 389-595 1.65e-07

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 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: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 53.24  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  389 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQtgacYKSLP--SRNGPLAVIVCPGWKKAQ 465
Cdd:cd17958     3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLaYLLPGFIHLD----LQPIPreQRNGPGVLVLTPTRELAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  466 FIFELLGEYSMssRPLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEvlfleane 545
Cdd:cd17958    79 QIEAECSKYSY--KGLKSVCVYGGGNRNEQIE-DLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768011969  546 qmfAILD-NFKKNIEVEERESAP-HQIVAVGVHWNKHIEHLIKEFMNDPYIV 595
Cdd:cd17958   148 ---RMLDmGFEPQIRKILLDIRPdRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 387-597 4.13e-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: 52.03  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSRNGPLAVIVCPGWKKAQ 465
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAaFIWPMLVHIMD---QRELEKGEGPIAVIVAPTRELAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  466 FIFELLGEYSMSSRpLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEVLF-LEAN 544
Cdd:cd17952    78 QIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFdMGFE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768011969  545 EQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPyIVIT 597
Cdd:cd17952   156 YQVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDP-IRVV 197
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 59-107 6.54e-07

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: 47.13  E-value: 6.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768011969   59 EGQVCVVYCEELKCWCRAIVKSITSSadqYLAECFLVDFAKNIPVKSKK 107
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEVLSN---DKVEVFFVDYGNTETVPLSD 46
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 5-111 1.18e-06

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 48.91  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    5 LVLKIEDPGCFWVIIKgCSPFLDHDVdyqKLNSAMNDFYNSTCQDIEIKPltlEEGQVCVVYCEELKCWCRAIVKSItsS 84
Cdd:cd20408     2 TVTEFKNPGEFYIQIY-TLEVLESLV---KLTSQLKKTYASVNNHKEYIP---EVGEVCVAKYSEDQNWYRALVQTV--D 72

                          90       100
                  ....*....|....*....|....*....
gi 768011969   85 ADQYLAECFLVDF--AKNIPVKSKKPAKK 111
Cdd:cd20408    73 VQQKKAGVFYIDYgnEETVPLNRIQPLKK 101
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 387-539 1.94e-06

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: 49.88  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTGacyKSLPSRNGPLAVIVCPGWKKAQ 465
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLaFLIPVLEILLKR---KANLKKGQVGALIISPTRELAT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768011969  466 FIFELLGEY-SMSSRPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLACQSLL--FLRLCHLILDEVEVL 539
Cdd:cd17960    78 QIYEVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKvkVKSLEVLVLDEADRL 154
TUDOR pfam00567
Tudor domain;
873-964 3.76e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 47.35  E-value: 3.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   873 YATLNAEMNEYFKDSNKTTVE-KVEKFGLYGLAEKTLFHRVQVLEVNQKEDAwalddiLVEFIDEGRTGLVTRDQLLHLP 951
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEDGKWYRAKITESLDDGLV------EVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 768011969   952 EHFHTLPPQAVEF 964
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 429-566 6.60e-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: 48.86  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  429 YLLPVLTVLQTGACYKSLPSRNGPLAVIVCPGWKKAQFIFEllgEYSMSSRPLH-PVLLTIGLHKEEAKNTKLPRGCDVI 507
Cdd:cd17945    44 FLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQQIEE---ETQKFAKPLGiRVVSIVGGHSIEEQAFSLRNGCEIL 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  508 VTTPYSLLRLLACQSLLFLRLCHLILDEVE-VLFLEANEQMFAILDNFKKNIEVEERESA 566
Cdd:cd17945   121 IATPGRLLDCLERRLLVLNQCTYVVLDEADrMIDMGFEPQVTKILDAMPVSNKKPDTEEA 180
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 387-574 9.93e-06

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: 48.13  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  387 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSR--NGPLAVIVCPGWKK 463
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLtYLLPIIQRLLR---YKLLAEGpfNAPRGLVITPSREL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  464 AQFIFEL---LGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRgCDVIVTTPYSLLRLLACQ--SLLFLRlcHLILDEVEV 538
Cdd:cd17948    78 AEQIGSVaqsLTEGL----GLKVKVITGGRTKRQIRNPHFEE-VDILVATPGALSKLLTSRiySLEQLR--HLVLDEADT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 768011969  539 LFLEA-NEQMFAILDNF---KKNIEVEERESAPHQIVAVG 574
Cdd:cd17948   151 LLDDSfNEKLSHFLRRFplaSRRSENTDGLDPGTQLVLVS 190
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 373-591 1.24e-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: 48.47  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  373 KPCLTIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSRNG 451
Cdd:cd18050    59 KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLaYLLPAIVHINH---QPYLERGDG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  452 PLAVIVCPGWKKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEeAKNTKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHL 531
Cdd:cd18050   136 PICLVLAPTRELAQQVQQVADDYGKSSR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYL 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768011969  532 ILDEVE-VLFLEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMND 591
Cdd:cd18050   214 VLDEADrMLDMGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 389-555 1.47e-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: 47.33  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  389 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCES-NPLLYLLPVLtvLQTGACYKSLP--SRNGPLAVIVCPGWKKAQ 465
Cdd:cd17951     3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSgKTLVFTLPLI--MFALEQEKKLPfiKGEGPYGLIVCPSRELAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  466 FIFELLGEYSMS-----SRPLHPVLLTIGLHKEEAKNTkLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVE-V 538
Cdd:cd17951    81 QTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEV-IRKGVHIVVATPGRLMDMLN-KKKINLDICrYLCLDEADrM 158

                         170
                  ....*....|....*..
gi 768011969  539 LFLEANEQMFAILDNFK 555
Cdd:cd17951   159 IDMGFEEDIRTIFSYFK 175
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 406-560 2.05e-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: 46.08  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   406 SWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQtgacykslPSRNGPLAVIVCPGWKKAQFIFELLGEYSmsSR 479
Cdd:pfam00270    7 AIPAILEGRDVLVQA-----PtgsgktLAFLLPALEALD--------KLDNGPQALVLAPTRELAEQIYEELKKLG--KG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   480 PLHPVLLTIGLHKEEAKNTKLpRGCDVIVTTPYSLLRLLAcQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNI 558
Cdd:pfam00270   72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAhRLLDMGFGPDLEEILRRLPKKR 149


                   ..
gi 768011969   559 EV 560
Cdd:pfam00270  150 QI 151
DEXDc smart00487
DEAD-like helicases superfamily;
441-596 1.01e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 44.79  E-value: 1.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    441 ACYKSLPSRNGPLAVIVCP------GWKKAqfiFELLGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSL 514
Cdd:smart00487   44 PALEALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRL 116

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969    515 LRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIeveeresaphQIVAVGVHWNKHIEHLIKEFMNDPY 593
Cdd:smart00487  117 LDLLENDKLSLSNVDLVILDEAhRLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPV 186


                    ...
gi 768011969    594 IVI 596
Cdd:smart00487  187 FID 189
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 1152-1252 1.36e-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: 42.49  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969 1152 HPQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVGDKF-YLADLELRGNIRKDDCQcVIRNDEPVITLAKERRE 1230
Cdd:cd00237     1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVkIYNEIELYDRVDPNDSK-HKRTDRSILCCLRKGKE 79

                          90       100
                  ....*....|....*....|....*.
gi 768011969 1231 --AWCHLLRQR-NPN-VAFDFDHWED 1252
Cdd:cd00237    80 gvAWPRLTKEKaKPNwLSVDFDNWRD 105
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 383-557 2.35e-04

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 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: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 43.73  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  383 LSADLKKALQRNKFPGPSHTESYSWPPI-ARGCDVVVISHCESNPLL-YLLPVL-TVLQTgacyKSLPSRNGPLAVIVCP 459
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPIlSTGDDVLARAKTGTGKTLaFLLPAIqSLLNT----KPAGRRSGVSALIISP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  460 GWKKAQFIFEllgEYSMSSRPLHP--VLLTIG---LHKEEAKNTKlpRGCDVIVTTPYSLLRLLACQSLL--FLRLCHLI 532
Cdd:cd17964    77 TRELALQIAA---EAKKLLQGLRKlrVQSAVGgtsRRAELNRLRR--GRPDILVATPGRLIDHLENPGVAkaFTDLDYLV 151

                         170       180
                  ....*....|....*....|....*....
gi 768011969  533 LDEVEVL----FLEANEQMFAILDNFKKN 557
Cdd:cd17964   152 LDEADRLldmgFRPDLEQILRHLPEKNAD 180
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 11-96 2.39e-04

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: 42.62  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969   11 DPGCFWV-IIKGCSP----FLDHDVDYQKLNSAMNDFYNSTCQDIEIKplTLEEGQVCVVyCEELKCWCRAIVKSITSSA 85
Cdd:cd20435     1 DATHYSArILEHRSSdgevTKSMSSTYLKLSMKLNMYYSDPSNRILHG--KVKVGDLCAV-EDENNLYHRVKVLEITEKD 77

                          90
                  ....*....|....
gi 768011969   86 DQY---LAECFLVD 96
Cdd:cd20435    78 DKTkprEVLVKFID 91
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 929-977 3.14e-04

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: 41.24  E-value: 3.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768011969  929 ILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIE 977
Cdd:cd20418    35 ILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDSE 83
PTZ00424 PTZ00424
helicase 45; Provisional
 499-783 2.71e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  499 KLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIEVEE-RESAPHQIVavgvh 576
Cdd:PTZ00424  142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAdEMLSRGFKGQIYDVFKKLPPDVQVALfSATMPNEIL----- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  577 wnkhieHLIKEFMNDPYIVITAMEEAALYGNVQQVVHLCLECEKTSSLLQALDFIP-SQAqktLIFTCSVAETEIVCKVV 655
Cdd:PTZ00424  217 ------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKVDYLTKKM 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  656 ESSSIFCLKMHKEMIfnlQNVLEQWKKKLSSGSQIILALTDdcvpLLA----ITDATCVIHFSFPASPKVFGGRLycmsd 731
Cdd:PTZ00424  288 HERDFTVSCMHGDMD---QKDRDLIMREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIHRI----- 355

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768011969  732 hfhaeqGSPAEQGdKKAKSVLLLTEKDASHAVGVLRYLERADAKVPAELYEF 783
Cdd:PTZ00424  356 ------GRSGRFG-RKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 879-961 3.23e-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: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  879 EMNEYFKDSNKTTVEKVEKFGlyglaektlfhrvQVLEVNQKEDAW--------ALDDILVEFIDEGRTGLVTRDQLLHL 950
Cdd:cd20427     6 EMKEFYSKSSTAMCLRSPSVG-------------QLVAVKAEEDAWlraqvievEEDKVKVYYVDHGFSEVVERSKLFKL 72

                          90
                  ....*....|.
gi 768011969  951 PEHFHTLPPQA 961
Cdd:cd20427    73 NKQFYSLPFQA 83
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 383-551 4.22e-03

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 39.98  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  383 LSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLqtgacyKSLPSRNGPLAVIVCPGW 461
Cdd:cd17959     8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAaFLIPMIEKL------KAHSPTVGARALILSPTR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011969  462 KKAQFIFELLGEYSMSSRpLHPVLLTiGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEVLF- 540
Cdd:cd17959    82 ELALQTLKVTKELGKFTD-LRTALLV-GGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFe 159

                         170
                  ....*....|.
gi 768011969  541 LEANEQMFAIL 551
Cdd:cd17959   160 MGFAEQLHEIL 170
 
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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