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Conserved domains on  [gi|2462568612|ref|XP_054178562|]
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putative ATP-dependent RNA helicase TDRD12 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD12_rpt1 cd20434
first Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 4-165 3.13e-92

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: 294.33  E-value: 3.13e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434      1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   82 TSSADQYLAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLYCTKPVTLHIDFCRDSTDIVPAKKWDNAAIQYFQ 161
Cdd:cd20434     81 MSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQ 160


                   ....
gi 2462568612  162 NLLK 165
Cdd:cd20434    161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 897-1018 1.44e-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: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  897 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 964
Cdd:cd20435      1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  965 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 1018
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
417-839 4.14e-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: 4.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  417 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 490
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  491 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 567
Cdd:COG0513     71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  568 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 641
Cdd:COG0513    138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  642 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 717
Cdd:COG0513    210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  718 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 785
Cdd:COG0513    285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  786 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 839
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 ...
 1193-1297 4.36e-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: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612 1193 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1269
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462568612 1270 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1297
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; ...
 4-165 3.13e-92

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: 294.33  E-value: 3.13e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434      1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   82 TSSADQYLAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLYCTKPVTLHIDFCRDSTDIVPAKKWDNAAIQYFQ 161
Cdd:cd20434     81 MSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQ 160


                   ....
gi 2462568612  162 NLLK 165
Cdd:cd20434    161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 897-1018 1.44e-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: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  897 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 964
Cdd:cd20435      1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  965 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 1018
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
TUDOR pfam00567
Tudor domain;
10-128 2.31e-18

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 82.02  E-value: 2.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   10 EDPGCFWVIIKGCSPF----LDHDVDYQKLNSAMNDFYNstCQDIEIKPLTLEEGQVCVVYCEElkCWCRAIvksITSSA 85
Cdd:pfam00567    1 STIDVVVSHIESPSTFyiqpKSDSKKLEKLTEELQEYYA--SKPPESLPPAVGDGCVAAFSEDG--KWYRAK---ITESL 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462568612   86 DQYLAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLY 128
Cdd:pfam00567   74 DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
417-839 4.14e-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: 4.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  417 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 490
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  491 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 567
Cdd:COG0513     71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  568 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 641
Cdd:COG0513    138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  642 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 717
Cdd:COG0513    210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  718 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 785
Cdd:COG0513    285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  786 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 839
Cdd:COG0513    337 AEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 427-635 1.87e-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: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVIS-------HCesnpllYLLPVLTVLQTgacyKSLPSRNGPLAVIVCP 499
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAqtgsgktLA------FLLPILEKLLP----EPKKKGRGPQALVLAP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  500 GWKKAQFIFELLGEYSmSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVEV 578
Cdd:cd00268     71 TRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEADR 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568612  579 L----FLeanEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 635
Cdd:cd00268    148 MldmgFE---EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 1193-1297 4.36e-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: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612 1193 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1269
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462568612 1270 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1297
Cdd:cd06465     81 EYWPRLTKEkgKLPWLKVDFDKWVD--EDE 108
TUDOR pfam00567
Tudor domain;
913-1004 4.23e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.96  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  913 YATLNAEMNEYFKDSNKTTVE-KVEKFGLYGLAEKTLFHRVQVLEVNQKEDAwalddiLVEFIDEGRTGLVTRDQLLHLP 991
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEDGKWYRAKITESLDDGLV------EVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 2462568612  992 EHFHTLPPQAVEF 1004
Cdd:pfam00567  101 PELESLPPQAIKC 113
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 446-600 2.12e-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: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  446 SWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQtgacykslPSRNGPLAVIVCPGWKKAQFIFELLGEYSmsSR 519
Cdd:pfam00270    7 AIPAILEGRDVLVQA-----PtgsgktLAFLLPALEALD--------KLDNGPQALVLAPTRELAEQIYEELKKLG--KG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  520 PLHPVLLTIGLHKEEAKNTKLpRGCDVIVTTPYSLLRLLAcQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNI 598
Cdd:pfam00270   72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAhRLLDMGFGPDLEEILRRLPKKR 149


                   ..
gi 2462568612  599 EV 600
Cdd:pfam00270  150 QI 151
DEXDc smart00487
DEAD-like helicases superfamily;
481-636 1.23e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 44.79  E-value: 1.23e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   481 ACYKSLPSRNGPLAVIVCP------GWKKAqfiFELLGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSL 554
Cdd:smart00487   44 PALEALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRL 116

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   555 LRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIeveeresaphQIVAVGVHWNKHIEHLIKEFMNDPY 633
Cdd:smart00487  117 LDLLENDKLSLSNVDLVILDEAhRLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPV 186


                    ...
gi 2462568612   634 IVI 636
Cdd:smart00487  187 FID 189
PTZ00424 PTZ00424
helicase 45; Provisional
 539-823 2.85e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  539 KLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIEVEE-RESAPHQIVavgvh 616
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAdEMLSRGFKGQIYDVFKKLPPDVQVALfSATMPNEIL----- 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  617 wnkhieHLIKEFMNDPYIVITAMEEAALYGNVQQVVHLCLECEKTSSLLQALDFIP-SQAqktLIFTCSVAETEIVCKVV 695
Cdd:PTZ00424   217 ------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKVDYLTKKM 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  696 ESSSIFCLKMHKEMIfnlQNVLEQWKKKLSSGSQIILALTDdcvpLLA----ITDATCVIHFSFPASPKVFGGRLycmsd 771
Cdd:PTZ00424   288 HERDFTVSCMHGDMD---QKDRDLIMREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIHRI----- 355

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462568612  772 hfhaeqGSPAEQGdKKAKSVLLLTEKDASHAVGVLRYLERADAKVPAELYEF 823
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; ...
 4-165 3.13e-92

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: 294.33  E-value: 3.13e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612    4 LLVLKIEDPGCFWVIIKGCSPFL-DHDVDYQKLNSAMNDFYNSTCQDIE-IKPLTLEEGQVCVVYCEELKCWCRAIVKSI 81
Cdd:cd20434      1 IQVLKIEDPGCFWGRILKGSGDLvVNPEEYENLQDEMNQFYHKGYKDVEeIKPSTLEEGQVCVVFCEELKCWCRAVVESL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   82 TSSADQYLAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLYCTKPVTLHIDFCRDSTDIVPAKKWDNAAIQYFQ 161
Cdd:cd20434     81 MSSADDYLAECFLVDYAKYIPVKSKDIRVALEAFMKLPYRAKKFRLYGIKPVTLHVDLCEDKAKIVPARKWDSAAIQYFQ 160


                   ....
gi 2462568612  162 NLLK 165
Cdd:cd20434    161 NLLK 164
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 897-1018 1.44e-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: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  897 NATNYFGRIVDKHMDL----------YATLNAEMNEYFKD-SNKTTVEKVEKFGLYGLAEKT-LFHRVQVLEVNQKEDAW 964
Cdd:cd20435      1 DATHYSARILEHRSSDgevtksmsstYLKLSMKLNMYYSDpSNRILHGKVKVGDLCAVEDENnLYHRVKVLEITEKDDKT 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  965 ALDDILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIEW 1018
Cdd:cd20435     81 KPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
TUDOR pfam00567
Tudor domain;
10-128 2.31e-18

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 82.02  E-value: 2.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   10 EDPGCFWVIIKGCSPF----LDHDVDYQKLNSAMNDFYNstCQDIEIKPLTLEEGQVCVVYCEElkCWCRAIvksITSSA 85
Cdd:pfam00567    1 STIDVVVSHIESPSTFyiqpKSDSKKLEKLTEELQEYYA--SKPPESLPPAVGDGCVAAFSEDG--KWYRAK---ITESL 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462568612   86 DQYLAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLY 128
Cdd:pfam00567   74 DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
417-839 4.14e-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: 4.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  417 TIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQTGAcykslpsRN 490
Cdd:COG0513      3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQA-----QtgtgktAAFLLPLLQRLDPSR-------PR 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  491 GPLAVIVCPgwkkAQFI---FELLGEYSmssrPLHpVLLTIGLHKEEAKNTKLPRGCDVIVTTPYsllRLLAcqsllFLR 567
Cdd:COG0513     71 APQALILAPtrelALQVaeeLRKLAKYL----GLR-VATVYGGVSIGRQIRALKRGVDIVVATPG---RLLD-----LIE 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  568 LCHLILDEVEVLFL-EANEqMfaiLDN-FKKNIE-VEERESAPHQIV---AVgvhWNKHIEHLIKEFMNDPyIVITAMEE 641
Cdd:COG0513    138 RGALDLSGVETLVLdEADR-M---LDMgFIEDIErILKLLPKERQTLlfsAT---MPPEIRKLAKRYLKNP-VRIEVAPE 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  642 AALYGNVQQVVHLCLECEKTSSLLQALDFIPsqAQKTLIFTCSVAETEIVCKVVESSSIFCLKMHKEMIfnlQN----VL 717
Cdd:COG0513    210 NATAETIEQRYYLVDKRDKLELLRRLLRDED--PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLS---QGqrerAL 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  718 EQWKkklsSGS-QIILAlTDdcvplLA-----ITDATCVIHFSFPASPKVF----G--GRlycmsdhfhaeqgspaeqGD 785
Cdd:COG0513    285 DAFR----NGKiRVLVA-TD-----VAargidIDDVSHVINYDLPEDPEDYvhriGrtGR------------------AG 336

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568612  786 KKAKSVLLLTEKDASHavgvLRYLERAdAKVPAELYEFTAGVLEAKEDKKAGRP 839
Cdd:COG0513    337 AEGTAISLVTPDERRL----LRAIEKL-IGQKIEEEELPGFEPVEEKRLERLKP 385
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 427-635 1.87e-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: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVIS-------HCesnpllYLLPVLTVLQTgacyKSLPSRNGPLAVIVCP 499
Cdd:cd00268      1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAqtgsgktLA------FLLPILEKLLP----EPKKKGRGPQALVLAP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  500 GWKKAQFIFELLGEYSmSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVEV 578
Cdd:cd00268     71 TRELAMQIAEVARKLG-KGTGLKVAAI-YGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVkYLVLDEADR 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568612  579 L----FLeanEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 635
Cdd:cd00268    148 MldmgFE---EDVEKILSALPKD----------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 409-636 1.86e-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: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  409 RNKIKPCLTIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLT------VLQTGa 481
Cdd:cd18049     17 HNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLsYLLPAIVhinhqpFLERG- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  482 cykslpsrNGPLAVIVCPGWKKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEeAKNTKLPRGCDVIVTTPYSLLRLLACQ 561
Cdd:cd18049     96 --------DGPICLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAG 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568612  562 SLLFLRLCHLILDEVE-VLFLEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDpYIVI 636
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. ...
 1193-1297 4.36e-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: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612 1193 PQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVG--DKFYLADLELRGNIRKDDCQCVIRNDEPVITLAK-ERR 1269
Cdd:cd06465      1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGggGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKkEAG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462568612 1270 EAWCHLLRQ--RNPNVAFDFDHWEDceEDS 1297
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) ...
 427-635 8.52e-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: 8.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKAL-QRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQtgaCYKSLPSRN-GPLAVIVCPGWKK 503
Cdd:cd17949      1 LVSHLkSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLaYLLPIIQRLL---SLEPRVDRSdGTLALVLVPTREL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  504 AQFIFELLGEYSMSSRPLHPVLLtIGLHKEEAKNTKLPRGCDVIVTTPYSLL-RLLACQSLLFLRLCHLILDEVEVL--- 579
Cdd:cd17949     78 ALQIYEVLEKLLKPFHWIVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLldm 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568612  580 -FLEANEQMFAILDNFKKNIEVEERESAPHQIVAVGVHWNKHIEHLIKEFMNDP-YIV 635
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 ...
 429-635 6.43e-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: 6.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  429 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLT------VLQTGacykslpsrNGPLAVIVCPGW 501
Cdd:cd17966      3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLaFLLPAIVhinaqpPLERG---------DGPIVLVLAPTR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  502 KKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVE-VLF 580
Cdd:cd17966     74 ELAQQIQQEANKFGGSSR-LRNTCVYGGAPKGPQIR-DLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADrMLD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462568612  581 LEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPYIV 635
Cdd:cd17966    152 MGFEPQIRKIVDQIRPD----------RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 59-109 1.81e-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: 51.75  E-value: 1.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462568612   59 EGQVCVVYCEELKCWCRAIVKSITSSadqYLAECFLVDFAKNIPVKSKNIR 109
Cdd:cd20379      1 VGDLCAAKYEEDGKWYRARVLEVLSN---DKVEVFFVDYGNTETVPLSDLR 48
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 9-161 4.72e-08

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


Pssm-ID: 410493  Cd Length: 135  Bit Score: 53.28  E-value: 4.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612    9 IEDPGCFWVIIKgcspflDHDVDYQKLNSAMNDFYnSTCQDIEIKPLTLEEGQVCVVYCEElKCWCRAIVKSItssaDQY 88
Cdd:cd20422      9 VKDPSEFWIRLG------EHAVPFSKLMRSMTAFY-SQASKLDGVVLKPQPGQLCCAKWKE-DRYYRAIVTAV----KGK 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462568612   89 LAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLyctkpvtlhidfcrdsTDIVP-AKKWDNAAIQYFQ 161
Cdd:cd20422     77 MVEVFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCL----------------ADICPlGERWSPEAISAFK 134
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 469-593 9.61e-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: 9.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  469 YLLPVLTVLQTgacyksLPSRNGPLAVIVCPGWKKAQFIFELLGEYSMSSrPLHPVLLTIGLHKEEAKNTKLPRGCDVIV 548
Cdd:cd17957     44 FLIPILQKLGK------PRKKKGLRALILAPTRELASQIYRELLKLSKGT-GLRIVLLSKSLEAKAKDGPKSITKYDILV 116

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462568612  549 TTPYSLLRLLaCQSLLFLR-LCHLILDEVEVL----FLEANEQMFAILDN 593
Cdd:cd17957    117 STPLRLVFLL-KQGPIDLSsVEYLVLDEADKLfepgFREQTDEILAACTN 165
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 1197-1272 1.44e-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: 1.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462568612 1197 WFQKEDVVILKIRIRNV--KDYKCQYLRDRVVFSA-WVGDKFYLADLELRGNIRKDDCQCVIRNDEPVITLAKERREAW 1272
Cdd:cd06463      1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVkGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEW 79
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 429-635 1.71e-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: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  429 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQtgacYKSLP--SRNGPLAVIVCPGWKKAQ 505
Cdd:cd17958      3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLaYLLPGFIHLD----LQPIPreQRNGPGVLVLTPTRELAL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  506 FIFELLGEYSMssRPLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEvlfleane 585
Cdd:cd17958     79 QIEAECSKYSY--KGLKSVCVYGGGNRNEQIE-DLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD-------- 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462568612  586 qmfAILD-NFKKNIEVEERESAP-HQIVAVGVHWNKHIEHLIKEFMNDPYIV 635
Cdd:cd17958    148 ---RMLDmGFEPQIRKILLDIRPdRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 427-637 4.39e-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: 4.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSRNGPLAVIVCPGWKKAQ 505
Cdd:cd17952      1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAaFIWPMLVHIMD---QRELEKGEGPIAVIVAPTRELAQ 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  506 FIFELLGEYSMSSRpLHPVLLTIGLHKEEAKNtKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEVLF-LEAN 584
Cdd:cd17952     78 QIYLEAKKFGKAYN-LRVVAVYGGGSKWEQAK-ALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFdMGFE 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462568612  585 EQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMNDPyIVIT 637
Cdd:cd17952    156 YQVRSIVGHVRPD----------RQTLLFSATFKKKIEQLARDILSDP-IRVV 197
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 11-133 1.47e-06

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: 48.79  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   11 DPGCFWV-IIKGCSP----FLDHDVDYQKLNSAMNDFYNSTCQDIEIKplTLEEGQVCVVyCEELKCWCRAIVKSITSSA 85
Cdd:cd20435      1 DATHYSArILEHRSSdgevTKSMSSTYLKLSMKLNMYYSDPSNRILHG--KVKVGDLCAV-EDENNLYHRVKVLEITEKD 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462568612   86 DQY---LAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLYCTKPV 133
Cdd:cd20435     78 DKTkprEVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPV 128
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 5-134 2.01e-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: 48.52  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612    5 LVLKIEDPGCFWVIIKgCSPFLDHDVdyqKLNSAMNDFYNSTCQDIEIKPltlEEGQVCVVYCEELKCWCRAIVKSItsS 84
Cdd:cd20408      2 TVTEFKNPGEFYIQIY-TLEVLESLV---KLTSQLKKTYASVNNHKEYIP---EVGEVCVAKYSEDQNWYRALVQTV--D 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462568612   85 ADQYLAECFLVDF--AKNIPVKSknIRVVVESFMQLPYRAKKFSLYCTKPVT 134
Cdd:cd20408     73 VQQKKAGVFYIDYgnEETVPLNR--IQPLKKDIELFPPCAIKCCLANVKPPS 122
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 427-579 2.12e-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: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTGacyKSLPSRNGPLAVIVCPGWKKAQ 505
Cdd:cd17960      1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLaFLIPVLEILLKR---KANLKKGQVGALIISPTRELAT 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568612  506 FIFELLGEY-SMSSRPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLACQSLL--FLRLCHLILDEVEVL 579
Cdd:cd17960     78 QIYEVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKvkVKSLEVLVLDEADRL 154
TUDOR pfam00567
Tudor domain;
913-1004 4.23e-06

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 46.96  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  913 YATLNAEMNEYFKDSNKTTVE-KVEKFGLYGLAEKTLFHRVQVLEVNQKEDAwalddiLVEFIDEGRTGLVTRDQLLHLP 991
Cdd:pfam00567   27 LEKLTEELQEYYASKPPESLPpAVGDGCVAAFSEDGKWYRAKITESLDDGLV------EVLFIDYGNTETVPLSDLRPLP 100

                           90
                   ....*....|...
gi 2462568612  992 EHFHTLPPQAVEF 1004
Cdd:pfam00567  101 PELESLPPQAIKC 113
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 62-128 5.44e-06

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


Pssm-ID: 410494  Cd Length: 80  Bit Score: 45.55  E-value: 5.44e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568612   62 VCVVYCEELKCWCRAIVKSITSSADQylAECFLVDFAKNIPVKSKNIRVVVESFMQLPYRAKKFSLY 128
Cdd:cd20423      8 VCLAKYSEDGKWCRALIDNVYEPVEM--VEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLY 72
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 469-606 6.83e-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: 6.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  469 YLLPVLTVLQTGACYKSLPSRNGPLAVIVCPGWKKAQFIFEllgEYSMSSRPLH-PVLLTIGLHKEEAKNTKLPRGCDVI 547
Cdd:cd17945     44 FLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQQIEE---ETQKFAKPLGiRVVSIVGGHSIEEQAFSLRNGCEIL 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  548 VTTPYSLLRLLACQSLLFLRLCHLILDEVE-VLFLEANEQMFAILDNFKKNIEVEERESA 606
Cdd:cd17945    121 IATPGRLLDCLERRLLVLNQCTYVVLDEADrMIDMGFEPQVTKILDAMPVSNKKPDTEEA 180
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 427-614 1.03e-05

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: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  427 LKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSR--NGPLAVIVCPGWKK 503
Cdd:cd17948      1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLtYLLPIIQRLLR---YKLLAEGpfNAPRGLVITPSREL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  504 AQFIFEL---LGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRgCDVIVTTPYSLLRLLACQ--SLLFLRlcHLILDEVEV 578
Cdd:cd17948     78 AEQIGSVaqsLTEGL----GLKVKVITGGRTKRQIRNPHFEE-VDILVATPGALSKLLTSRiySLEQLR--HLVLDEADT 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462568612  579 LFLEA-NEQMFAILDNF---KKNIEVEERESAPHQIVAVG 614
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 ...
 413-631 1.34e-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: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  413 KPCLTIDSSPLSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLQTgacYKSLPSRNG 491
Cdd:cd18050     59 KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLaYLLPAIVHINH---QPYLERGDG 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  492 PLAVIVCPGWKKAQFIFELLGEYSMSSRpLHPVLLTIGLHKEeAKNTKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHL 571
Cdd:cd18050    136 PICLVLAPTRELAQQVQQVADDYGKSSR-LKSTCIYGGAPKG-PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYL 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568612  572 ILDEVE-VLFLEANEQMFAILDNFKKNieveeresapHQIVAVGVHWNKHIEHLIKEFMND 631
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 ...
 429-595 1.52e-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: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  429 KALQRNKFPGPSHTESYSWPPIARGCDVVVISHCES-NPLLYLLPVLtvLQTGACYKSLP--SRNGPLAVIVCPGWKKAQ 505
Cdd:cd17951      3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSgKTLVFTLPLI--MFALEQEKKLPfiKGEGPYGLIVCPSRELAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  506 FIFELLGEYSMS-----SRPLHPVLLTIGLHKEEAKNTkLPRGCDVIVTTPYSLLRLLAcQSLLFLRLC-HLILDEVE-V 578
Cdd:cd17951     81 QTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEV-IRKGVHIVVATPGRLMDMLN-KKKINLDICrYLCLDEADrM 158

                          170
                   ....*....|....*..
gi 2462568612  579 LFLEANEQMFAILDNFK 595
Cdd:cd17951    159 IDMGFEEDIRTIFSYFK 175
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 446-600 2.12e-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: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  446 SWPPIARGCDVVVIShcesnP------LLYLLPVLTVLQtgacykslPSRNGPLAVIVCPGWKKAQFIFELLGEYSmsSR 519
Cdd:pfam00270    7 AIPAILEGRDVLVQA-----PtgsgktLAFLLPALEALD--------KLDNGPQALVLAPTRELAEQIYEELKKLG--KG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  520 PLHPVLLTIGLHKEEAKNTKLpRGCDVIVTTPYSLLRLLAcQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNI 598
Cdd:pfam00270   72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAhRLLDMGFGPDLEEILRRLPKKR 149


                   ..
gi 2462568612  599 EV 600
Cdd:pfam00270  150 QI 151
DEXDc smart00487
DEAD-like helicases superfamily;
481-636 1.23e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 44.79  E-value: 1.23e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   481 ACYKSLPSRNGPLAVIVCP------GWKKAqfiFELLGEYSmssrPLHPVLLTIGLHKEEAKNTKLPRGCDVIVTTPYSL 554
Cdd:smart00487   44 PALEALKRGKGGRVLVLVPtrelaeQWAEE---LKKLGPSL----GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRL 116

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   555 LRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIeveeresaphQIVAVGVHWNKHIEHLIKEFMNDPY 633
Cdd:smart00487  117 LDLLENDKLSLSNVDLVILDEAhRLLDGGFGDQLEKLLKLLPKNV----------QLLLLSATPPEEIENLLELFLNDPV 186


                    ...
gi 2462568612   634 IVI 636
Cdd:smart00487  187 FID 189
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 1192-1292 1.46e-04

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


Pssm-ID: 107218  Cd Length: 106  Bit Score: 42.49  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612 1192 HPQIKWFQKEDVVILKIRIRNVKDYKCQYLRDRVVFSAWVGDKF-YLADLELRGNIRKDDCQcVIRNDEPVITLAKERRE 1270
Cdd:cd00237      1 PAKTLWYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDNVkIYNEIELYDRVDPNDSK-HKRTDRSILCCLRKGKE 79

                           90       100
                   ....*....|....*....|....*.
gi 2462568612 1271 --AWCHLLRQR-NPN-VAFDFDHWED 1292
Cdd:cd00237     80 gvAWPRLTKEKaKPNwLSVDFDNWRD 105
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 423-597 2.43e-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: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  423 LSADLKKALQRNKFPGPSHTESYSWPPI-ARGCDVVVISHCESNPLL-YLLPVL-TVLQTgacyKSLPSRNGPLAVIVCP 499
Cdd:cd17964      1 LDPSLLKALTRMGFETMTPVQQKTLKPIlSTGDDVLARAKTGTGKTLaFLLPAIqSLLNT----KPAGRRSGVSALIISP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  500 GWKKAQFIFEllgEYSMSSRPLHP--VLLTIG---LHKEEAKNTKlpRGCDVIVTTPYSLLRLLACQSLL--FLRLCHLI 572
Cdd:cd17964     77 TRELALQIAA---EAKKLLQGLRKlrVQSAVGgtsRRAELNRLRR--GRPDILVATPGRLIDHLENPGVAkaFTDLDYLV 151

                          170       180
                   ....*....|....*....|....*....
gi 2462568612  573 LDEVEVL----FLEANEQMFAILDNFKKN 597
Cdd:cd17964    152 LDEADRLldmgFRPDLEQILRHLPEKNAD 180
Tudor_TDRD7_rpt3 cd20429
third Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 31-122 2.66e-04

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: 41.32  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612   31 DYQKLNSAMND---FYNSTcqdiEIKPLTLEEGQVCVVYCEELkcWCRAIVKSITSSAdqyLAECFLVDFAKNIPVKSKN 107
Cdd:cd20429      5 ELHKLEVLMEEmilYYNKT----EERPVAIEKNKVYAAKIENN--WYRVLVKGILTNG---LVSVYELDYGKHELVSIRK 75

                           90
                   ....*....|....*
gi 2462568612  108 IRVVVESFMQLPYRA 122
Cdd:cd20429     76 VQPLIEKFRQLPFQA 90
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 969-1017 3.40e-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: 3.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462568612  969 ILVEFIDEGRTGLVTRDQLLHLPEHFHTLPPQAVEFIVCRVKPADNEIE 1017
Cdd:cd20418     35 ILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDSE 83
PTZ00424 PTZ00424
helicase 45; Provisional
 539-823 2.85e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 41.74  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  539 KLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEV-EVLFLEANEQMFAILDNFKKNIEVEE-RESAPHQIVavgvh 616
Cdd:PTZ00424   142 KLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAdEMLSRGFKGQIYDVFKKLPPDVQVALfSATMPNEIL----- 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  617 wnkhieHLIKEFMNDPYIVITAMEEAALYGNVQQVVHLCLECEKTSSLLQALDFIP-SQAqktLIFTCSVAETEIVCKVV 695
Cdd:PTZ00424   217 ------ELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTiTQA---IIYCNTRRKVDYLTKKM 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  696 ESSSIFCLKMHKEMIfnlQNVLEQWKKKLSSGSQIILALTDdcvpLLA----ITDATCVIHFSFPASPKVFGGRLycmsd 771
Cdd:PTZ00424   288 HERDFTVSCMHGDMD---QKDRDLIMREFRSGSTRVLITTD----LLArgidVQQVSLVINYDLPASPENYIHRI----- 355

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462568612  772 hfhaeqGSPAEQGdKKAKSVLLLTEKDASHAVGVLRYLERADAKVPAELYEF 823
Cdd:PTZ00424   356 ------GRSGRFG-RKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 919-1001 3.30e-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: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  919 EMNEYFKDSNKTTVEKVEKFGlyglaektlfhrvQVLEVNQKEDAW--------ALDDILVEFIDEGRTGLVTRDQLLHL 990
Cdd:cd20427      6 EMKEFYSKSSTAMCLRSPSVG-------------QLVAVKAEEDAWlraqvievEEDKVKVYYVDHGFSEVVERSKLFKL 72

                           90
                   ....*....|.
gi 2462568612  991 PEHFHTLPPQA 1001
Cdd:cd20427     73 NKQFYSLPFQA 83
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 423-591 4.36e-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: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  423 LSADLKKALQRNKFPGPSHTESYSWPPIARGCDVVVISHCESNPLL-YLLPVLTVLqtgacyKSLPSRNGPLAVIVCPGW 501
Cdd:cd17959      8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAaFLIPMIEKL------KAHSPTVGARALILSPTR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568612  502 KKAQFIFELLGEYSMSSRpLHPVLLTiGLHKEEAKNTKLPRGCDVIVTTPYSLLRLLACQSLLFLRLCHLILDEVEVLF- 580
Cdd:cd17959     82 ELALQTLKVTKELGKFTD-LRTALLV-GGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFe 159

                          170
                   ....*....|.
gi 2462568612  581 LEANEQMFAIL 591
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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