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Conserved domains on  [gi|21355075|ref|NP_649767|]
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uncharacterized protein Dmel_CG7878 [Drosophila melanogaster]

Protein Classification

KH domain-containing protein; DEAD/DEAH box helicase family protein( domain architecture ID 13610392)

K homology (KH) domain-containing protein may bind single-stranded RNA or DNA| DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
174-663 7.94e-163

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


The actual alignment was detected with superfamily member PTZ00110:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 545  Bit Score: 480.04  E-value: 7.94e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  174 RYDGGGYDRYKGNSYEFNPTSSESNKDN---------GDLTGIIDWEALNKAsiaataarwskcpPLTKNFYKEAPEVAN 244
Cdd:PTZ00110  36 NYQANHQDNYGGFRPGYGNYSGGYGGFGmnsygsstlGKRLQPIDWKSINLV-------------PFEKNFYKEHPEVSA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  245 LTKSEIERIREENnKITVSyvfepkEGETsppIPNPVWTFEqcFAEYPD-MLEEITKMGFSKPSPIQSQAWPILLQGHDM 323
Cdd:PTZ00110 103 LSSKEVDEIRKEK-EITII------AGEN---VPKPVVSFE--YTSFPDyILKSLKNAGFTEPTPIQVQGWPIALSGRDM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  324 IGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQIEMEVKKY--SFRgMKAVCVYGGGNRNMQI 400
Cdd:PTZ00110 171 IGIAETGSGKTLAFLLPAIVHINAQ--PLLRYGdGPIVLVLAPTRELAEQIREQCNKFgaSSK-IRNTVAYGGVPKRGQI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  401 SDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQ 480
Cdd:PTZ00110 248 YALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLAR 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  481 SYMKN-PIQVCVGSLDLAATHSVKQIIKLMEDDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCI 559
Cdd:PTZ00110 328 DLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  560 HGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWA 639
Cdd:PTZ00110 408 HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
                        490       500
                 ....*....|....*....|....
gi 21355075  640 MAKELIEILQEAEQEVPDELHNMA 663
Cdd:PTZ00110 488 LARDLVKVLREAKQPVPPELEKLS 511
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
92-152 7.87e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


:

Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 55.37  E-value: 7.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075    92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL-----DKCDLIVKITGSiQSNVIDAINHVRK 152
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIppsesEGNERIVTITGT-PEAVEAAKALIEE 65
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
174-663 7.94e-163

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 480.04  E-value: 7.94e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  174 RYDGGGYDRYKGNSYEFNPTSSESNKDN---------GDLTGIIDWEALNKAsiaataarwskcpPLTKNFYKEAPEVAN 244
Cdd:PTZ00110  36 NYQANHQDNYGGFRPGYGNYSGGYGGFGmnsygsstlGKRLQPIDWKSINLV-------------PFEKNFYKEHPEVSA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  245 LTKSEIERIREENnKITVSyvfepkEGETsppIPNPVWTFEqcFAEYPD-MLEEITKMGFSKPSPIQSQAWPILLQGHDM 323
Cdd:PTZ00110 103 LSSKEVDEIRKEK-EITII------AGEN---VPKPVVSFE--YTSFPDyILKSLKNAGFTEPTPIQVQGWPIALSGRDM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  324 IGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQIEMEVKKY--SFRgMKAVCVYGGGNRNMQI 400
Cdd:PTZ00110 171 IGIAETGSGKTLAFLLPAIVHINAQ--PLLRYGdGPIVLVLAPTRELAEQIREQCNKFgaSSK-IRNTVAYGGVPKRGQI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  401 SDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQ 480
Cdd:PTZ00110 248 YALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLAR 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  481 SYMKN-PIQVCVGSLDLAATHSVKQIIKLMEDDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCI 559
Cdd:PTZ00110 328 DLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  560 HGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWA 639
Cdd:PTZ00110 408 HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
                        490       500
                 ....*....|....*....|....
gi 21355075  640 MAKELIEILQEAEQEVPDELHNMA 663
Cdd:PTZ00110 488 LARDLVKVLREAKQPVPPELEKLS 511
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
288-673 4.73e-159

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 465.39  E-value: 4.73e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 288 FAEY---PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRgganVLVLA 364
Cdd:COG0513   4 FADLglsPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-LLQRLDPSRPRAPQ----ALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 365 PTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML 443
Cdd:COG0513  79 PTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 444 DMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAAThSVKQIIkLMEDDMDKFNTITSFV 523
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRY-YLVDKRDKLELLRRLL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 524 KNMSsTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVIN 603
Cdd:COG0513 237 RDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355075 604 YDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIEILQE--AEQEVPDELHNMARRFKAMKDKR 673
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLKPKI 387
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
294-490 1.99e-136

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: 398.76  E-value: 1.99e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTPRGTRGGANVLVLAPTRELALQI 373
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 374 EMEVKKYSFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRK 453
Cdd:cd17958  81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21355075 454 VMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVC 490
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
307-478 3.94e-56

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: 188.61  E-value: 3.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   307 SPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTeyqstpRGTRGGANVLVLAPTRELALQIEMEVKKY-SFRGM 385
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   386 KAVCVYGGGNRNMQISDLeRGAEIIICTPGRLNDLImANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTI 465
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 21355075   466 MTSATWPPGVRRL 478
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
298-505 3.49e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 179.22  E-value: 3.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075    298 ITKMGFSKPSPIQSQAWPILLQG-HDMIGIAQTGTGKTLAFLLPgmIHTEYQSTPRGTrgganVLVLAPTRELALQIEME 376
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP--ALEALKRGKGGR-----VLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075    377 VKKY-SFRGMKAVCVYGGGNRNMQISDLERG-AEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKV 454
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21355075    455 MLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLaatHSVKQI 505
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL---EPIEQF 201
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
92-152 7.87e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 55.37  E-value: 7.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075    92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL-----DKCDLIVKITGSiQSNVIDAINHVRK 152
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIppsesEGNERIVTITGT-PEAVEAAKALIEE 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
93-151 1.34e-08

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 51.53  E-value: 1.34e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL-----IVKITGSiQSNVIDAINHVR 151
Cdd:cd00105   1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEgsgerVVTITGT-PEAVEKAKELIE 63
KH smart00322
K homology RNA-binding domain;
90-154 7.75e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.60  E-value: 7.75e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075     90 DFSESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL---IVKITGSiQSNVIDAINHVRKQV 154
Cdd:smart00322   2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSeerVVEITGP-PENVEKAAELILEIL 68
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
434-625 9.41e-06

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 48.22  E-value: 9.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   434 LVLDEADRMLD--MGFepqIRKVMLDIRPDRQTIM-TSATWPPGVRRLAQSyMKNPIQVCVGSLDLAATHSVKQIIKLME 510
Cdd:TIGR01587 128 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEK-IGYVEFNEPLDLKEERRFENHRFILIES 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   511 DDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDG--FMTQCIHGNRDQMDREQAIADI-----KSGVVRIL 583
Cdd:TIGR01587 204 DKVGEISSLERLLEFIKKGGSIAIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAKKEAELlremkKSNEKFVI 283
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21355075   584 VATDVASRGLDIeDITHVINYDFPhnIEEYVHRVGRTGRAGR 625
Cdd:TIGR01587 284 VATQVIEASLDI-SADVMITELAP--IDSLIQRLGRLHRYGR 322
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
93-150 8.45e-03

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 39.26  E-value: 8.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075   93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKcDLIVKITGSIQSNVIDAINHV 150
Cdd:PRK11824 556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED-DGTVKIAATDGEAAEAAKERI 612
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
174-663 7.94e-163

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 480.04  E-value: 7.94e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  174 RYDGGGYDRYKGNSYEFNPTSSESNKDN---------GDLTGIIDWEALNKAsiaataarwskcpPLTKNFYKEAPEVAN 244
Cdd:PTZ00110  36 NYQANHQDNYGGFRPGYGNYSGGYGGFGmnsygsstlGKRLQPIDWKSINLV-------------PFEKNFYKEHPEVSA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  245 LTKSEIERIREENnKITVSyvfepkEGETsppIPNPVWTFEqcFAEYPD-MLEEITKMGFSKPSPIQSQAWPILLQGHDM 323
Cdd:PTZ00110 103 LSSKEVDEIRKEK-EITII------AGEN---VPKPVVSFE--YTSFPDyILKSLKNAGFTEPTPIQVQGWPIALSGRDM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  324 IGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQIEMEVKKY--SFRgMKAVCVYGGGNRNMQI 400
Cdd:PTZ00110 171 IGIAETGSGKTLAFLLPAIVHINAQ--PLLRYGdGPIVLVLAPTRELAEQIREQCNKFgaSSK-IRNTVAYGGVPKRGQI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  401 SDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQ 480
Cdd:PTZ00110 248 YALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLAR 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  481 SYMKN-PIQVCVGSLDLAATHSVKQIIKLMEDDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCI 559
Cdd:PTZ00110 328 DLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  560 HGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWA 639
Cdd:PTZ00110 408 HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
                        490       500
                 ....*....|....*....|....
gi 21355075  640 MAKELIEILQEAEQEVPDELHNMA 663
Cdd:PTZ00110 488 LARDLVKVLREAKQPVPPELEKLS 511
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
288-673 4.73e-159

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 465.39  E-value: 4.73e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 288 FAEY---PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRgganVLVLA 364
Cdd:COG0513   4 FADLglsPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-LLQRLDPSRPRAPQ----ALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 365 PTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML 443
Cdd:COG0513  79 PTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 444 DMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAAThSVKQIIkLMEDDMDKFNTITSFV 523
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRY-YLVDKRDKLELLRRLL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 524 KNMSsTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVIN 603
Cdd:COG0513 237 RDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355075 604 YDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIEILQE--AEQEVPDELHNMARRFKAMKDKR 673
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLKPKI 387
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
294-490 1.99e-136

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: 398.76  E-value: 1.99e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTPRGTRGGANVLVLAPTRELALQI 373
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 374 EMEVKKYSFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRK 453
Cdd:cd17958  81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21355075 454 VMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVC 490
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
294-489 2.70e-97

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: 298.13  E-value: 2.70e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQ 372
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ--PPLERGdGPIVLVLAPTRELAQQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKYSFR-GMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQI 451
Cdd:cd17966  79 IQQEANKFGGSsRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21355075 452 RKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
294-489 1.45e-95

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: 293.58  E-value: 1.45e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGM--IHTEYQSTPRGTRgganVLVLAPTRELAL 371
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQ----ALVLAPTRELAM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQ 450
Cdd:cd00268  77 QIAEVARKLGkGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEED 156
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21355075 451 IRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd00268 157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
292-652 1.80e-93

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 297.87  E-value: 1.80e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLpGMIHteyQSTPRgtRGGANVLVLAPTRELAL 371
Cdd:PRK11776  13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGL-GLLQ---KLDVK--RFRVQALVLCPTRELAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  372 QIEMEVKKYSfRGM---KAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFE 448
Cdd:PRK11776  87 QVAKEIRRLA-RFIpniKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  449 PQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDlaATHSVKQIIKLMEDDmDKFNTITSFVKNM-- 526
Cdd:PRK11776 166 DAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPD-ERLPALQRLLLHHqp 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  527 SSTdkiIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDF 606
Cdd:PRK11776 243 ESC---VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 21355075  607 PHNIEEYVHRVGRTGRAGRQGTSISFFTREDwaMAK-ELIEILQEAE 652
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEE--MQRaNAIEDYLGRK 364
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
292-631 4.77e-87

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 280.93  E-value: 4.77e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIH-TEYQSTPRGTRGgANVLVLAPTRELA 370
Cdd:PRK10590  10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPHAKGRRP-VRALILTPTRELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  371 LQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:PRK10590  89 AQIGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  450 QIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDlAATHSVKQIIKLMedDMDKFNTITSFVKNMSST 529
Cdd:PRK10590 169 DIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFV--DKKRKRELLSQMIGKGNW 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  530 DKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHN 609
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
                        330       340
                 ....*....|....*....|..
gi 21355075  610 IEEYVHRVGRTGRAGRQGTSIS 631
Cdd:PRK10590 326 PEDYVHRIGRTGRAAATGEALS 347
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
288-632 1.53e-83

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 271.05  E-value: 1.53e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  288 FAEY---PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHteYQSTPRGTRGGANVLVLA 364
Cdd:PRK11192   3 FSELeldESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQH--LLDFPRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  365 PTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML 443
Cdd:PRK11192  81 PTRELAMQVADQARELAkHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  444 DMGFEPQIRKVMLDIRPDRQTIMTSATWP-PGVRRLAQSYMKNPIQVcvgsldlAATHSVKQIIKLME-----DDMD-KF 516
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV-------EAEPSRRERKKIHQwyyraDDLEhKT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  517 NTITSFVKNMSSTdKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIE 596
Cdd:PRK11192 234 ALLCHLLKQPEVT-RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 21355075  597 DITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISF 632
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
277-489 5.33e-83

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 261.93  E-value: 5.33e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 277 IPNPVWTFEQC-FAEypDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQStPRGTR 355
Cdd:cd17953   7 CPKPIQKWSQCgLSE--KVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQR-PVKPG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 356 GGANVLVLAPTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMAN---VIDVSTI 431
Cdd:cd17953  84 EGPIGLIMAPTRELALQIYVECKKFSkALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANngrVTNLRRV 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075 432 TYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17953 164 TYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
224-492 5.55e-83

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: 263.79  E-value: 5.55e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 224 RW--SKCPPLTKNFYKEAPEVANLTKSEIERIREENnKITVSYVFEPKegetsppipnPVWTFEQcfAEYPD-MLEEITK 300
Cdd:cd18050  13 KWdlSELPKFEKNFYVEHPEVARMTQYDVEELRRKK-EITIRGVGCPK----------PVFAFHQ--ANFPQyVMDVLLD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 301 MGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQIEMEVKK 379
Cdd:cd18050  80 QNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ--PYLERGdGPICLVLAPTRELAQQVQQVADD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 380 Y--SFRgMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLD 457
Cdd:cd18050 158 YgkSSR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21355075 458 IRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVG 492
Cdd:cd18050 237 IRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
292-492 2.26e-79

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 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: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 252.41  E-value: 2.26e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIH---TEYQSTPRGTRGGAN--VLVLAPT 366
Cdd:cd17967   9 ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLP-IISkllEDGPPSVGRGRRKAYpsALILAPT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 367 RELALQIEMEVKKYSFR-GMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDM 445
Cdd:cd17967  88 RELAIQIYEEARKFSYRsGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDM 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21355075 446 GFEPQIRKVML--DIRP--DRQTIMTSATWPPGVRRLAQSYMKNPIQVCVG 492
Cdd:cd17967 168 GFEPQIRKIVEhpDMPPkgERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
285-646 3.90e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 258.75  E-value: 3.90e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  285 EQCFAE---YPDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTPRGTR-GGANV 360
Cdd:PRK04837   7 EQKFSDfalHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKvNQPRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  361 LVLAPTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEA 439
Cdd:PRK04837  87 LIMAPTRELAVQIHADAEPLAqATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  440 DRMLDMGFEPQIRkVMLDIRPD---RQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAAtHSVKQII--KLMEDDMD 514
Cdd:PRK04837 167 DRMFDLGFIKDIR-WLFRRMPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTG-HRIKEELfyPSNEEKMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  515 KFNTITSfvknMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLD 594
Cdd:PRK04837 245 LLQTLIE----EEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21355075  595 IEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTrEDWAMAKELIE 646
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAC-EEYALNLPAIE 371
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
216-637 7.29e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 259.84  E-value: 7.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  216 ASIAATAARWSKCPPLTKNFYKEAP--EVANLTKSEIERIREENNKITVS------YVFEPKEGETSppipnpvwtFEQc 287
Cdd:PRK01297  22 PSPAAAPAPPPPAKTAAPATKAAAPaaAAPRAEKPKKDKPRRERKPKPASlwkledFVVEPQEGKTR---------FHD- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  288 FAEYPDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgmIHTEYQSTP---RGTRGGANVLVLA 364
Cdd:PRK01297  92 FNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLIS--IINQLLQTPppkERYMGEPRALIIA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  365 PTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLE-RGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRM 442
Cdd:PRK01297 170 PTRELVVQIAKDAAALTkYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRM 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  443 LDMGFEPQIRKVMLDIRP--DRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAaTHSVKQIIKLMEDDmDKFNTIT 520
Cdd:PRK01297 250 LDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVA-SDTVEQHVYAVAGS-DKYKLLY 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  521 SFVKNmSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITH 600
Cdd:PRK01297 328 NLVTQ-NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 21355075  601 VINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTRED 637
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
278-493 1.47e-78

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: 250.70  E-value: 1.47e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 278 PNPVWTFEQcfAEYP-DMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG 356
Cdd:cd18049  20 PKPVLNFYE--ANFPaNVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ--PFLERG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 357 -GANVLVLAPTRELALQIEMEVKKYSFRG-MKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYL 434
Cdd:cd18049  96 dGPICLVLAPTRELAQQVQQVAAEYGRACrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYL 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355075 435 VLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGS 493
Cdd:cd18049 176 VLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
284-632 2.42e-74

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 252.08  E-value: 2.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  284 FEQCFAEY---PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGM--IHTEYQStprgtrggA 358
Cdd:PRK11634   4 FETTFADLglkAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnLDPELKA--------P 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  359 NVLVLAPTRELALQIEMEVKKYS--FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVL 436
Cdd:PRK11634  76 QILVLAPTRELAVQVAEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  437 DEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSL-----DLAATHSVKQiiklmed 511
Cdd:PRK11634 156 DEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvttrpDISQSYWTVW------- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  512 DMDKFNTITSFVKnMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASR 591
Cdd:PRK11634 229 GMRKNEALVRFLE-AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAAR 307
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 21355075  592 GLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISF 632
Cdd:PRK11634 308 GLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
294-489 5.30e-73

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: 234.62  E-value: 5.30e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQstPRGTRG-GANVLVLAPTRELALQ 372
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ--RELEKGeGPIAVIVAPTRELAQQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKYSFR-GMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQI 451
Cdd:cd17952  79 IYLEAKKFGKAyNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21355075 452 RKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
215-673 2.26e-72

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 243.93  E-value: 2.26e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  215 KASIAATAARWSKCPPLTKNFYKEAPEVAN-LTKSEIERIREennKITVSYvfepkEGETSPPipnPVWTFEQC-FAeyP 292
Cdd:PLN00206  64 KSRVAVGAPKPKRLPATDECFYVRDPGSTSgLSSSQAELLRR---KLEIHV-----KGEAVPP---PILSFSSCgLP--P 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  293 DMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIH-TEYQSTPRGTRGGANVLVLAPTRELAL 371
Cdd:PLN00206 131 KLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcCTIRSGHPSEQRNPLAMVLTPTRELCV 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  372 QIEMEVKKYSfRGM--KAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:PLN00206 211 QVEDQAKVLG-KGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRD 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  450 QIRKVMLDIrPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDlAATHSVKQIIKLMEDDMDK---FNTITSFVKNM 526
Cdd:PLN00206 290 QVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPN-RPNKAVKQLAIWVETKQKKqklFDILKSKQHFK 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  527 SStdkIIIFCGRKVRADDLSSELTL-DGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYD 605
Cdd:PLN00206 368 PP---AVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFD 444
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355075  606 FPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIEILQEAEQEVPDELHN---MARRFKAMKDKR 673
Cdd:PLN00206 445 MPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELANsryLGSGRKRKKKRR 515
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
294-489 6.16e-70

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: 227.59  E-value: 6.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRGGAN---VLVLAPTRELA 370
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIP-LLVYISRLPPLDEETKDDgpyALILAPTRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 371 LQIEMEVKKY-SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:cd17945  80 QQIEEETQKFaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 450 QIRKVM-----LDIRPD---------------RQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17945 160 QVTKILdampvSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
288-658 1.05e-67

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 232.92  E-value: 1.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  288 FAEYPDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLL---------PGMIHTEYQStPRGtrgga 358
Cdd:PRK04537  14 FDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALADRKPED-PRA----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  359 nvLVLAPTRELALQIEMEVKKY-SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMAN-VIDVSTITYLVL 436
Cdd:PRK04537  88 --LILAPTRELAIQIHKDAVKFgADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHkVVSLHACEICVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  437 DEADRMLDMGFEPQIRKVM--LDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAATHsVKQIIKLMEDDmd 514
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLrrMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPADE-- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  515 kfNTITSFVKNMSSTD--KIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRG 592
Cdd:PRK04537 243 --EKQTLLLGLLSRSEgaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075  593 LDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTrEDWAMAkeLIEILQEAEQEVPDE 658
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFAC-ERYAMS--LPDIEAYIEQKIPVE 383
PTZ00424 PTZ00424
helicase 45; Provisional
293-659 2.66e-67

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 226.63  E-value: 2.66e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  293 DMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTprgtrgGANVLVLAPTRELALQ 372
Cdd:PTZ00424  38 DLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN------ACQALILAPTRELAQQ 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  373 IEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQI 451
Cdd:PTZ00424 112 IQKVVLALGdYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQI 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  452 RKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLAaTHSVKQIIKLMEDDMDKFNTITSFVKNMSSTdK 531
Cdd:PTZ00424 192 YDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELT-LEGIRQFYVAVEKEEWKFDTLCDLYETLTIT-Q 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  532 IIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIE 611
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 21355075  612 EYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIEILQEAEQEVPDEL 659
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEV 397
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
273-484 7.11e-66

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 218.30  E-value: 7.11e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 273 TSPPIPNPVWTFEQcfAEYPDML-EEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLP---GMIHTEYQ 348
Cdd:cd18052  34 TGRNPPPAILTFEE--ANLCETLlKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMKEGLT 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 349 STPRGTRGGANVLVLAPTRELALQIEMEVKKYSFRGM-KAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVID 427
Cdd:cd18052 112 ASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCiRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355075 428 VSTITYLVLDEADRMLDMGFEPQIRKVMLDI----RPDRQTIMTSATWPPGVRRLAQSYMK 484
Cdd:cd18052 192 LSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
273-492 1.94e-59

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 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: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 200.65  E-value: 1.94e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 273 TSPPIPNPVWTFEQCfaeypdMLEEITKMG-----FSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLP--GMIHT 345
Cdd:cd18051  12 TGENCPPHIETFSDL------DLGEIIRNNielarYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilSQIYE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 346 E--YQSTPRGTRGGAN------VLVLAPTRELALQIEMEVKKYSFRGMKAVCV-YGGGNRNMQISDLERGAEIIICTPGR 416
Cdd:cd18051  86 QgpGESLPSESGYYGRrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVvYGGADIGQQMRDLERGCHLLVATPGR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 417 LNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRK-VMLDIRP---DRQTIMTSATWPPGVRRLAQSYMKNPIQVCVG 492
Cdd:cd18051 166 LVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRiVEQDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
292-484 6.91e-59

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: 197.81  E-value: 6.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQ-GHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRGGANVLVLAPTRELA 370
Cdd:cd17964   3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLP-AIQSLLNTKPAGRRSGVSALIISPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 371 LQIEMEVKK--YSFRGMKAVCVYGGGNRNMQISDLER-GAEIIICTPGRLNDLIMANV--IDVSTITYLVLDEADRMLDM 445
Cdd:cd17964  82 LQIAAEAKKllQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGvaKAFTDLDYLVLDEADRLLDM 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21355075 446 GFEPQIRKvMLDIRPD-----RQTIMTSATWPPGVRRLAQSYMK 484
Cdd:cd17964 162 GFRPDLEQ-ILRHLPEknadpRQTLLFSATVPDEVQQIARLTLK 204
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
307-478 3.94e-56

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: 188.61  E-value: 3.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   307 SPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTeyqstpRGTRGGANVLVLAPTRELALQIEMEVKKY-SFRGM 385
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   386 KAVCVYGGGNRNMQISDLeRGAEIIICTPGRLNDLImANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTI 465
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 21355075   466 MTSATWPPGVRRL 478
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
299-487 1.53e-54

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: 186.25  E-value: 1.53e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 299 TKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRG-GANVLVLAPTRELALQIEMEV 377
Cdd:cd17949   7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLP-IIQRLLSLEPRVDRSdGTLALVLVPTRELALQIYEVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 378 KKY--SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLND-LIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKV 454
Cdd:cd17949  86 EKLlkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21355075 455 M--LDIRPD-----------RQTIMTSATWPPGVRRLAQSYMKNPI 487
Cdd:cd17949 166 LelLDDKRSkaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
295-492 1.97e-54

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: 185.10  E-value: 1.97e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 295 LEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHteyQSTPRGTRGGANVLVLAPTRELALQIE 374
Cdd:cd17957   2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIP-ILQ---KLGKPRKKKGLRALILAPTRELASQIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 375 MEVKKYSFRGMKAVCVYGGGNRNMQISDLE--RGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIR 452
Cdd:cd17957  78 RELLKLSKGTGLRIVLLSKSLEAKAKDGPKsiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21355075 453 KVMLDIR-PDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVG 492
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
502-633 8.04e-54

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 181.17  E-value: 8.04e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 502 VKQIIKLMEDDmDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVR 581
Cdd:cd18787   1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21355075 582 ILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFF 633
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
286-489 2.44e-53

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: 182.50  E-value: 2.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 286 QCFAEYPDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPR-GTRGganvLVLA 364
Cdd:cd17959   4 QSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIP-MIEKLKAHSPTvGARA----LILS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 365 PTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML 443
Cdd:cd17959  79 PTRELALQTLKVTKELGkFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21355075 444 DMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEXDc smart00487
DEAD-like helicases superfamily;
298-505 3.49e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 179.22  E-value: 3.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075    298 ITKMGFSKPSPIQSQAWPILLQG-HDMIGIAQTGTGKTLAFLLPgmIHTEYQSTPRGTrgganVLVLAPTRELALQIEME 376
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP--ALEALKRGKGGR-----VLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075    377 VKKY-SFRGMKAVCVYGGGNRNMQISDLERG-AEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKV 454
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21355075    455 MLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCVGSLDLaatHSVKQI 505
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL---EPIEQF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
294-490 7.42e-51

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 175.52  E-value: 7.42e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGM---IHTEYQStpRGTRgganVLVLAPTRELA 370
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILerlLYRPKKK--AATR----VLVLVPTRELA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 371 LQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIM-ANVIDVSTITYLVLDEADRMLDMGFE 448
Cdd:cd17947  75 MQCFSVLQQLAqFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFA 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21355075 449 PQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVC 490
Cdd:cd17947 155 DELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
292-490 8.92e-51

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 175.58  E-value: 8.92e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRgtrggANVLVLAPTRELAL 371
Cdd:cd17954   9 EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP-ILQALLENPQR-----FFALVLAPTRELAQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKY-SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLND-LIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:cd17954  83 QISEQFEALgSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDFEP 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21355075 450 QIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVC 490
Cdd:cd17954 163 EIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
288-489 4.93e-48

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 167.86  E-value: 4.93e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 288 FAEY---PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLP--GMIHTEyqstprgtRGGANVLV 362
Cdd:cd17940   1 FEDYglkRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPilEKIDPK--------KDVIQALI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 363 LAPTRELALQIEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADR 441
Cdd:cd17940  73 LVPTRELALQTSQVCKELGkHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADK 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21355075 442 MLDMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17940 153 LLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
295-489 3.56e-47

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: 165.44  E-value: 3.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 295 LEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRGGANVLVLAPTRELALQIE 374
Cdd:cd17960   2 LDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP-VLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 375 mEV----KKYSFRGMKAVCVYGGGNRNMQISDLER-GAEIIICTPGRLNDLI--MANVIDVSTITYLVLDEADRMLDMGF 447
Cdd:cd17960  81 -EVlqsfLEHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsrKADKVKVKSLEVLVLDEADRLLDLGF 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21355075 448 EPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
294-489 7.02e-46

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: 162.12  E-value: 7.02e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPG-MIHTEYQ-STPRGTRGGANVLVLAPTRELAL 371
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEkKLPFIKGEGPYGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKYS-------FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLD 444
Cdd:cd17951  81 QTHEVIEYYCkalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21355075 445 MGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
294-489 1.21e-44

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 158.48  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIH-TEYQSTPrgtrggaNVLVLAPTRELALQ 372
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcLTEHRNP-------SALILTPTRELAVQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKYsFRG---MKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:cd17962  74 IEDQAKEL-MKGlppMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQ 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21355075 450 QIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17962 153 QVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
292-489 5.19e-44

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) 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: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 156.58  E-value: 5.19e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQG--HDMIGIAQTGTGKTLAFLLpGM---IHTEYQSTprgtrggaNVLVLAPT 366
Cdd:cd17963   3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVL-AMlsrVDPTLKSP--------QALCLAPT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 367 RELALQIEMEVKKY-SFRGMKAVCVYGGG--NRNMQISdlergAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML 443
Cdd:cd17963  74 RELARQIGEVVEKMgKFTGVKVALAVPGNdvPRGKKIT-----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21355075 444 DM-GFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17963 149 DTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
302-491 7.38e-44

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 156.30  E-value: 7.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 302 GFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQStpRGTRG-GANVLVLAPTRELALQIEMEVKKY 380
Cdd:cd17941   9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVP-LLEKLYRE--RWTPEdGLGALIISPTRELAMQIFEVLRKV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 381 -SFRGMKAVCVYGGgnRNMQIsDLERGAE--IIICTPGRLNDLIMANV-IDVSTITYLVLDEADRMLDMGFEPQIRKVML 456
Cdd:cd17941  86 gKYHSFSAGLIIGG--KDVKE-EKERINRmnILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21355075 457 DIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCV 491
Cdd:cd17941 163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
295-489 3.40e-42

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 151.74  E-value: 3.40e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 295 LEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPG--MIHTeYQSTPrgtRGGANVLVLAPTRELALQ 372
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLYK-LKFKP---RNGTGVIIISPTRELALQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKYSFRGMKAV-CVYGGGNRNMQISDLERGAEIIICTPGRLND-LIMANVIDVSTITYLVLDEADRMLDMGFEPQ 450
Cdd:cd17942  78 IYGVAKELLKYHSQTFgIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21355075 451 IRKVMLDIRPDRQTIMTSATWPPGVRRLAQ-SYMKNPIQV 489
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
295-486 5.28e-42

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 151.22  E-value: 5.28e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 295 LEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTEYQStPRGTRGganvLVLAPTRELALQIE 374
Cdd:cd17955  11 VKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSED-PYGIFA----LVLTPTRELAYQIA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 375 MEVKKY-SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANV---IDVSTITYLVLDEADRMLDMGFEPQ 450
Cdd:cd17955  85 EQFRALgAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDdttKVLSRVKFLVLDEADRLLTGSFEDD 164
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21355075 451 IRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNP 486
Cdd:cd17955 165 LATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
295-489 7.92e-42

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 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: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 150.49  E-value: 7.92e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 295 LEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMihteyQSTPRGTRGgANVLVLAPTRELALQIE 374
Cdd:cd17943   2 LEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-----ESLDLERRH-PQVLILAPTREIAVQIH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 375 MEVKKY--SFRGMKaVCVYGGGNRNMQisDLER--GAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQ 450
Cdd:cd17943  76 DVFKKIgkKLEGLK-CEVFIGGTPVKE--DKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21355075 451 IRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17943 153 VNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
294-470 3.26e-39

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 144.69  E-value: 3.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWP-ILLQGHDMIGIAQTGTGKTLAFLLPgMIH---TEYQSTPRGT-RGGANVLVLAPTRE 368
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIP-ILErllSQKSSNGVGGkQKPLRALILTPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 369 LALQIE---MEVKKYSfrGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMAN---VIDVSTITYLVLDEADRM 442
Cdd:cd17946  80 LAVQVKdhlKAIAKYT--NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRM 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21355075 443 LDMG-FEP--QIRKVMLDIRP----DRQTIMTSAT 470
Cdd:cd17946 158 LEKGhFAEleKILELLNKDRAgkkrKRQTFVFSAT 192
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
292-487 4.25e-39

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 143.49  E-value: 4.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHT--EYQSTpRGTRGGANVLVLAPTREL 369
Cdd:cd17961   3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP-IIQKilKAKAE-SGEEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 370 ALQIEMEVKK---YSFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMA-NVIDVSTITYLVLDEADRMLDM 445
Cdd:cd17961  81 AQQVSKVLEQltaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21355075 446 GFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPI 487
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
293-489 1.66e-38

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins 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: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 141.31  E-value: 1.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 293 DMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLpgMIHTEYQSTPRGTRgganVLVLAPTRELALQ 372
Cdd:cd17939   7 DLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSI--GALQRIDTTVRETQ----ALVLAPTRELAQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKY-SFRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQI 451
Cdd:cd17939  81 IQKVVKALgDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21355075 452 RKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
292-489 3.67e-38

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are 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: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 140.66  E-value: 3.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGM--IHTEYQSTprgtrggaNVLVLAPTREL 369
Cdd:cd18046   8 ESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILqqIDTSLKAT--------QALVLAPTREL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 370 ALQIE---MEVKKYsfrgMKAVC--VYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLD 444
Cdd:cd18046  80 AQQIQkvvMALGDY----MGIKChaCIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21355075 445 MGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
308-484 1.91e-37

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 138.44  E-value: 1.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 308 PIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGM--IHTEYQSTPRGTrgGANVLVLAPTRELALQIEMEVKKYSfRGM 385
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPRKRGR--APKVLVLAPTRELANQVTKDFKDIT-RKL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 386 KAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVM-----LDIRP 460
Cdd:cd17944  92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSED 171
                       170       180
                ....*....|....*....|....
gi 21355075 461 DRQTIMTSATWPPGVRRLAQSYMK 484
Cdd:cd17944 172 NPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
292-491 3.83e-35

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 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: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 132.47  E-value: 3.83e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQStprgtrGGANVLVLAPTRELAL 371
Cdd:cd17950  11 PELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVSVLVICHTRELAF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKYS--FRGMKAVCVYGGGNRNMQISDLERGA-EIIICTPGRLNDLIMANVIDVSTITYLVLDEADRML-DMGF 447
Cdd:cd17950  85 QISNEYERFSkyMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDM 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21355075 448 EPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQVCV 491
Cdd:cd17950 165 RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
292-489 7.42e-33

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 125.51  E-value: 7.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 292 PDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHTeyqstprgtrggANVLVLAPTRELAL 371
Cdd:cd17938   8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQI------------VVALILEPSRELAE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKYS--FRGMKAVC--VYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGF 447
Cdd:cd17938  75 QTYNCIENFKkyLDNPKLRValLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGN 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21355075 448 EPQIRKVMLDI-----RPDR-QTIMTSATW-PPGVRRLAQSYMKNPIQV 489
Cdd:cd17938 155 LETINRIYNRIpkitsDGKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
293-489 2.56e-32

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 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: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 124.12  E-value: 2.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 293 DMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLpGMIHTeYQSTPRGTRgganVLVLAPTRELALQ 372
Cdd:cd18045   9 DLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSI-SVLQC-LDIQVRETQ----ALILSPTRELAVQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 373 IEMEVKKYS-FRGMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEPQI 451
Cdd:cd18045  83 IQKVLLALGdYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQI 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21355075 452 RKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNPIQV 489
Cdd:cd18045 163 YDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
514-624 3.86e-31

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 117.31  E-value: 3.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   514 DKFNTITSFVKNmSSTDKIIIFCGRKVRADdLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGL 593
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 21355075   594 DIEDITHVINYDFPHNIEEYVHRVGRTGRAG 624
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
294-478 6.75e-29

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: 115.16  E-value: 6.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPgMIHT--EYQSTPRGTRGGANVLVLAPTRELAL 371
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQRllRYKLLAEGPFNAPRGLVITPSRELAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 372 QIEMEVKKYSFR-GMKAVCVyGGGNRNMQISDLERG-AEIIICTPGRLNDLIMANVIDVSTITYLVLDEADRMLDMGFEP 449
Cdd:cd17948  80 QIGSVAQSLTEGlGLKVKVI-TGGRTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21355075 450 QIRKVM----LDIRPDR---------QTIMTSATWPPGVRRL 478
Cdd:cd17948 159 KLSHFLrrfpLASRRSEntdgldpgtQLVLVSATMPSGVGEV 200
HELICc smart00490
helicase superfamily c-terminal domain;
543-624 4.05e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.29  E-value: 4.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075    543 DDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGR 622
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 21355075    623 AG 624
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
294-448 1.31e-23

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 100.01  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITKMGFSKPSPIQSQAWPILLQG---------HDMIGIAQTGTGKTLAFLLPgMIHTEYQSTPRGTRgganVLVLA 364
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLP-IVQALSKRVVPRLR----ALIVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 365 PTRELALQIEMEVKKYSfRGMKAVCVYGGGNRN-----MQISDLERG-----AEIIICTPGRLNDLIMANV-IDVSTITY 433
Cdd:cd17956  76 PTKELVQQVYKVFESLC-KGTGLKVVSLSGQKSfkkeqKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPgFTLKHLRF 154
                       170
                ....*....|....*
gi 21355075 434 LVLDEADRMLDMGFE 448
Cdd:cd17956 155 LVIDEADRLLNQSFQ 169
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
281-486 2.33e-20

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) 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: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 90.47  E-value: 2.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 281 VWTFEQCFAEyPDMLEEITKMGFSKPSPIQSQAWPILLQG--HDMIGIAQTGTGKTLAFLLPGMIHTEYQST-PRgtrgg 357
Cdd:cd18048  17 VKSFEELHLK-EELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLyPQ----- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 358 anVLVLAPTRELALQIEMEVKKysfrgMKAVCV-----YG-GGNRNMQISDLErgAEIIICTPGRLNDLIMA-NVIDVST 430
Cdd:cd18048  91 --CLCLSPTFELALQTGKVVEE-----MGKFCVgiqviYAiRGNRPGKGTDIE--AQIVIGTPGTVLDWCFKlRLIDVTN 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21355075 431 ITYLVLDEADRMLDM-GFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNP 486
Cdd:cd18048 162 ISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
320-470 2.59e-18

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 82.07  E-value: 2.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 320 GHDMIGIAQTGTGKTLAFLLPgMIHteyqstpRGTRGGANVLVLAPTRELALQIEMEVKKYSFRGMKAVCVYGGGNRNMQ 399
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLA-ALL-------LLLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEER 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355075 400 ISDLERGAEIIICTPGRLNDLIMANV-IDVSTITYLVLDEADRMLDMGFE-----PQIRKVMLdirPDRQTIMTSAT 470
Cdd:cd00046  73 EKNKLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGalildLAVRKAGL---KNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
317-671 3.11e-18

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 88.27  E-value: 3.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 317 LLQGHDMIGIAQTGTGKTLAFLLPGMIhteyqstprgtRGGAnVLVLAPTreLALqieME--VKKYSFRGMKAVCVYGGG 394
Cdd:COG0514  29 VLAGRDALVVMPTGGGKSLCYQLPALL-----------LPGL-TLVVSPL--IAL---MKdqVDALRAAGIRAAFLNSSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 395 NRNMQ---ISDLERGA-EIIICTPGRLNDLIMANVIDVSTITYLVLDEA--------DrmldmgFEP---QIRKVmLDIR 459
Cdd:COG0514  92 SAEERrevLRALRAGElKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD------FRPdyrRLGEL-RERL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 460 PDRQTIMTSATWPPGVRR--LAQSYMKNPiQVCVGSLD-----LaathsvkQIIKLMEDDmdKFNTITSFVKNMSStDKI 532
Cdd:COG0514 165 PNVPVLALTATATPRVRAdiAEQLGLEDP-RVFVGSFDrpnlrL-------EVVPKPPDD--KLAQLLDFLKEHPG-GSG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 533 IIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATdVA-SRGLDIEDITHVINYDFPHNIE 611
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIE 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355075 612 EYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIeilqeaEQEVPDELHNMARRFK--AMKD 671
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI------EQSPPDEERKRVERAKldAMLA 368
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
283-486 6.07e-18

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 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: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 82.85  E-value: 6.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 283 TFEQCFAEyPDMLEEITKMGFSKPSPIQSQAWPILLQG--HDMIGIAQTGTGKTLAFLLPGMIHTEYQSTprgtrgGANV 360
Cdd:cd18047   2 SFEELRLK-PQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANK------YPQC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 361 LVLAPTRELALQIEMEVKK-----------YSFRGMKAvcvygggNRNMQISDlergaEIIICTPGRLND-LIMANVIDV 428
Cdd:cd18047  75 LCLSPTYELALQTGKVIEQmgkfypelklaYAVRGNKL-------ERGQKISE-----QIVIGTPGTVLDwCSKLKFIDP 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355075 429 STITYLVLDEADRML-DMGFEPQIRKVMLDIRPDRQTIMTSATWPPGVRRLAQSYMKNP 486
Cdd:cd18047 143 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
294-479 2.77e-17

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 82.04  E-value: 2.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 294 MLEEITK-----MGFSKPSPIQSQAWPILLQ-----------GHD------MIGiAQTGTGKTLAFLLPGM-------IH 344
Cdd:cd17965  14 IIKEILKgsnktDEEIKPSPIQTLAIKKLLKtlmrkvtkqtsNEEpklevfLLA-AETGSGKTLAYLAPLLdylkrqeQE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 345 TEYQSTP----RGTRGGANVLVLAPTRELALQIEMEVKKYS-FRGMK-AVCVYGGGNRNMQISDLERGA-EIIICTPGRL 417
Cdd:cd17965  93 PFEEAEEeyesAKDTGRPRSVILVPTHELVEQVYSVLKKLShTVKLGiKTFSSGFGPSYQRLQLAFKGRiDILVTTPGKL 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355075 418 NDLIMANVIDVSTITYLVLDEADRMLDMGFEPQIRKVMLDIRPDRQTIMTSATWP-----------PGVRRLA 479
Cdd:cd17965 173 ASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPkefdktlrklfPDVVRIA 245
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
329-633 7.73e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.31  E-value: 7.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 329 TGTGKTLAFLLpgmihteyqsTPRGTRGGANVLVLAPTRELALQIEMEVKKYSfrgmkAVCVYGGGNRnmqisdlERGAE 408
Cdd:COG1061 109 TGTGKTVLALA----------LAAELLRGKRVLVLVPRRELLEQWAEELRRFL-----GDPLAGGGKK-------DSDAP 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 409 IIICTPGRLNDLIMANVIDvSTITYLVLDEADRmldmGFEPQIRKVMLDIRPDRqTIMTSATwpP----GVRRLAQSYMK 484
Cdd:COG1061 167 ITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAY-RLGLTAT--PfrsdGREILLFLFDG 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 485 npiqvCVGSLDLA--------ATHSVKQIIKLMEDDMDKFNTITSFVKN-------------------MSSTDKIIIFCG 537
Cdd:COG1061 239 -----IVYEYSLKeaiedgylAPPEYYGIRVDLTDERAEYDALSERLREalaadaerkdkilrellreHPDDRKTLVFCS 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 538 RKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRV 617
Cdd:COG1061 314 SVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRL 393
                       330
                ....*....|....*.
gi 21355075 618 GRTGRAGRQGTSISFF 633
Cdd:COG1061 394 GRGLRPAPGKEDALVY 409
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
308-439 7.88e-11

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 61.51  E-value: 7.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 308 PIQSQAW-PILLQGHDMIGIAQTGTGKTLAFLLpGMIHteyqstpRGTRGGANVLVLAPTRELALQIEMEVKKySFRGMK 386
Cdd:cd17921   4 PIQREALrALYLSGDSVLVSAPTSSGKTLIAEL-AILR-------ALATSGGKAVYIAPTRALVNQKEADLRE-RFGPLG 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21355075 387 AVCVYGGGNRNMQISDLERgAEIIICTP----GRLNDLIMANVIDVstiTYLVLDEA 439
Cdd:cd17921  75 KNVGLLTGDPSVNKLLLAE-ADILVATPekldLLLRNGGERLIQDV---RLVVVDEA 127
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
92-152 7.87e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 55.37  E-value: 7.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075    92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL-----DKCDLIVKITGSiQSNVIDAINHVRK 152
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIppsesEGNERIVTITGT-PEAVEAAKALIEE 65
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
530-624 1.00e-09

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 55.40  E-value: 1.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 530 DKIIIFCGRKVRADDLSSELTldgfmtqcihgnrdqmdreqaiadiksgvvrILVATDVASRGLDIEDITHVINYDFPHN 609
Cdd:cd18785   4 VKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSS 52
                        90
                ....*....|....*
gi 21355075 610 IEEYVHRVGRTGRAG 624
Cdd:cd18785  53 AASYIQRVGRAGRGG 67
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
515-618 1.97e-09

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 56.33  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 515 KFNTITSFVKNM-SSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIK--SGVVRILVATDVASR 591
Cdd:cd18793  12 KLEALLELLEELrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGV 91
                        90       100       110
                ....*....|....*....|....*....|...
gi 21355075 592 GLDIEDITHVINYDFPHN--IEEY----VHRVG 618
Cdd:cd18793  92 GLNLTAANRVILYDPWWNpaVEEQaidrAHRIG 124
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
533-623 6.97e-09

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 54.90  E-value: 6.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 533 IIFCGRKVRADDLSS-----ELTLDGFMTQCI--HGNRDQ-----MDR---EQAIADIKSGVVRILVATDVASRGLDIED 597
Cdd:cd18802  29 IIFVERRATAVVLSRllkehPSTLAFIRCGFLigRGNSSQrkrslMTQrkqKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                        90       100
                ....*....|....*....|....*.
gi 21355075 598 ITHVINYDFPHNIEEYVHRVGRtGRA 623
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
530-633 1.29e-08

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 53.75  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 530 DKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHN 609
Cdd:cd18794  31 GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKS 110
                        90       100
                ....*....|....*....|....
gi 21355075 610 IEEYVHRVGRTGRAGRQGTSISFF 633
Cdd:cd18794 111 MESYYQESGRAGRDGLPSECILFY 134
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
93-151 1.34e-08

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 51.53  E-value: 1.34e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL-----IVKITGSiQSNVIDAINHVR 151
Cdd:cd00105   1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEgsgerVVTITGT-PEAVEKAKELIE 63
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
495-627 4.11e-08

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.66  E-value: 4.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 495 DLAATHSVKQIIKLMED-DMD--KFNTITSFVKNMSST---DKIIIFCGRKVRADDLSSELTLDG-----FMTQcihGNR 563
Cdd:COG1111 313 RLVSDPRFRKAMRLAEEaDIEhpKLSKLREILKEQLGTnpdSRIIVFTQYRDTAEMIVEFLSEPGikagrFVGQ---ASK 389
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355075 564 D------QMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYD-FPHNIeEYVHRVGRTGRaGRQG 627
Cdd:COG1111 390 EgdkgltQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGR-KREG 458
KH smart00322
K homology RNA-binding domain;
90-154 7.75e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.60  E-value: 7.75e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075     90 DFSESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL---IVKITGSiQSNVIDAINHVRKQV 154
Cdd:smart00322   2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSeerVVEITGP-PENVEKAAELILEIL 68
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
248-630 1.31e-07

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 54.84  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 248 SEIERIREENNKITVSYVFEPKEGETSPpIPNPVwtfeqcfaeYPDMLEEITKMGFSKPSPIQSQAWPILLQGHDMIGIA 327
Cdd:COG1205   9 ERLRASPRYGDQIVHVRTIPAREARYAP-WPDWL---------PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIAT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 328 QTGTGKTLAFLLPGMihTEYQSTPRGTrgganVLVLAPT-----------RELALQIEMEVKkysfrgmkaVCVYGG--- 393
Cdd:COG1205  79 PTASGKSLAYLLPVL--EALLEDPGAT-----ALYLYPTkalardqlrrlRELAEALGLGVR---------VATYDGdtp 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 394 -GNRnmqiSDLERGAEIIICTPGRLNDLIMANVID----VSTITYLVLDEA---------------DRML----DMGFEP 449
Cdd:COG1205 143 pEER----RWIREHPDIVLTNPDMLHYGLLPHHTRwarfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDP 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 450 QIrkvmldirpdrqtIMTSATW-----------------------PPGVRRLAqsyMKNPIQVCVGsLDLAATHSVKQII 506
Cdd:COG1205 219 QF-------------ILASATIgnpaehaerltgrpvtvvdedgsPRGERTFV---LWNPPLVDDG-IRRSALAEAARLL 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 507 K-LMEDDMdkfNTITsFVKNMSSTDKIIIFCGRKVRADDLSSEltldgfmtqcIHGNRDQM---DREQAIADIKSGVVRI 582
Cdd:COG1205 282 AdLVREGL---RTLV-FTRSRRGAELLARYARRALREPDLADR----------VAAYRAGYlpeERREIERGLRSGELLG 347
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21355075 583 LVAT-------DVAsrGLDIedithVINYDFPHNIEEYVHRVGRTGRAGRQGTSI 630
Cdd:COG1205 348 VVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
91-154 1.87e-07

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 48.80  E-value: 1.87e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075  91 FSESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDLIVK--ITGSiQSNVIDAINHVRKQV 154
Cdd:cd22449   4 YTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEGNveIKGS-KKNVEEAKKRILSQI 68
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
93-147 2.93e-07

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 47.95  E-value: 2.93e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL---IVKITGSiQSNVIDAI 147
Cdd:cd02394   4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEAnsdEIRIEGS-PEGVKKAK 60
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
318-441 3.01e-07

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 51.66  E-value: 3.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 318 LQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTPRGTRgganVLVLAPTRELALQiEMEVKKYSFR--GMKAVCVYGGGN 395
Cdd:cd17927  15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK----VVFLANKVPLVEQ-QKEVFRKHFErpGYKVTGLSGDTS 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21355075 396 RNMQISDLERGAEIIICTPGRL-NDLIMANVIDVSTITYLVLDEADR 441
Cdd:cd17927  90 ENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHN 136
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
302-654 3.31e-07

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 53.56  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  302 GFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIhteyqstprgtRGGANvLVLAPTRELalqIEMEVKKYS 381
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV-----------LDGLT-LVVSPLISL---MKDQVDQLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  382 FRGMKAVCVYGGGNRNMQISDLERgaeiiiCTPGRLN-------DLIMANVIDVST---ITYLVLDEADRMLDMG--FEP 449
Cdd:PRK11057  87 ANGVAAACLNSTQTREQQLEVMAG------CRTGQIKllyiapeRLMMDNFLEHLAhwnPALLAVDEAHCISQWGhdFRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  450 ------QIRKVMldirPDRQTIMTSATWPPGVRR--LAQSYMKNPIqVCVGSLD-------LAATHS-VKQIIKLMEDDM 513
Cdd:PRK11057 161 eyaalgQLRQRF----PTLPFMALTATADDTTRQdiVRLLGLNDPL-IQISSFDrpnirytLVEKFKpLDQLMRYVQEQR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  514 DKFNtitsfvknmsstdkiIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSGVVRILVATDVASRGL 593
Cdd:PRK11057 236 GKSG---------------IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGI 300
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355075  594 DIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFFTREDWAMAKELIEILQEAEQE 654
Cdd:PRK11057 301 NKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQ 361
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
523-627 1.66e-06

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 48.12  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 523 VKNMSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCI----HGNR------DQMDREQAIADIKSGVVRILVATDVASRG 592
Cdd:cd18801  24 KKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEG 103
                        90       100       110
                ....*....|....*....|....*....|....*
gi 21355075 593 LDIEDITHVINYDFPHNIEEYVHRVGRTGRaGRQG 627
Cdd:cd18801 104 LDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
560-633 2.60e-06

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 47.64  E-value: 2.60e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355075 560 HGNRDQMDREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGRQGTSISFF 633
Cdd:cd18796  75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
310-441 3.75e-06

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 47.89  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 310 QSQAWPILLQGHDMIgIAQTGTGKTLAFLLpgmihteyQSTPRGTRGGANVLVLAPTRELALQIEMEVKKYSFRGMKAVC 389
Cdd:cd18035   7 QVLIAAVALNGNTLI-VLPTGLGKTIIAIL--------VAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITS 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21355075 390 VYGGGNRNMQiSDLERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADR 441
Cdd:cd18035  78 LTGEVKPEER-AERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
300-486 5.19e-06

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 47.90  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 300 KMGFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIhteyqsTPRGTrgganvLVLAPTRELalqIEMEVKK 379
Cdd:cd18016  12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV------SPGVT------VVISPLRSL---IVDQVQK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 380 YSFRGMKAVCVYG--GGNRNMQI-SDLERGAEII---------ICTPGRLNDlIMANVIDVSTITYLVLDEADRMLDMG- 446
Cdd:cd18016  77 LTSLDIPATYLTGdkTDAEATKIyLQLSKKDPIIkllyvtpekISASNRLIS-TLENLYERKLLARFVIDEAHCVSQWGh 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21355075 447 -FEPQIRKV-MLDIR-PDRQTIMTSATWPPGVRR--LAQSYMKNP 486
Cdd:cd18016 156 dFRPDYKRLnMLRQKfPSVPMMALTATATPRVQKdiLNQLKMLRP 200
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
91-154 5.76e-06

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 44.50  E-value: 5.76e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075  91 FSESLSIASEMVGKVIGRGGSNISRIQNDFNVRV----KLDKCDLIVKITGSiQSNVIDAINHVRKQV 154
Cdd:cd22417   1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIqfpdKGDENDDEITITGY-EKNAEAAKDAILKIV 67
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
434-625 9.41e-06

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 48.22  E-value: 9.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   434 LVLDEADRMLD--MGFepqIRKVMLDIRPDRQTIM-TSATWPPGVRRLAQSyMKNPIQVCVGSLDLAATHSVKQIIKLME 510
Cdd:TIGR01587 128 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEK-IGYVEFNEPLDLKEERRFENHRFILIES 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   511 DDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDG--FMTQCIHGNRDQMDREQAIADI-----KSGVVRIL 583
Cdd:TIGR01587 204 DKVGEISSLERLLEFIKKGGSIAIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAKKEAELlremkKSNEKFVI 283
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21355075   584 VATDVASRGLDIeDITHVINYDFPhnIEEYVHRVGRTGRAGR 625
Cdd:TIGR01587 284 VATQVIEASLDI-SADVMITELAP--IDSLIQRLGRLHRYGR 322
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
329-439 1.11e-05

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.88  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 329 TGTGKTL--AFLLPGMIHTEYQSTPRGTRgganVLVLAPTRELALQIEMEVKKYS-FRGMKavcVYGGGNRNMQISD--- 402
Cdd:cd18034  25 TGSGKTLiaVMLIKEMGELNRKEKNPKKR----AVFLVPTVPLVAQQAEAIRSHTdLKVGE---YSGEMGVDKWTKErwk 97
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21355075 403 -LERGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEA 439
Cdd:cd18034  98 eELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
95-138 1.11e-05

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. 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.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 43.43  E-value: 1.11e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21355075  95 LSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKC--DLIVKITGS 138
Cdd:cd22430   4 FKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGgqEAEVKIFGS 49
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
97-150 3.51e-05

first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411863 [Multi-domain]  Cd Length: 73  Bit Score: 42.14  E-value: 3.51e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355075  97 IASEMVGKVIGRGGSNISRIQNDFNVRVKLDK--------CDLIVKITGSIqSNVIDAINHV 150
Cdd:cd22435   8 VPNYAAGSIIGKGGQTIAQLQKETGARIKLSKnndfypgtTERVCLIQGEV-EAVNAVLDFI 68
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
434-625 4.33e-05

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 46.27  E-value: 4.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 434 LVLDEADRMLD--MGFepqIRKVMLDIRPDRQTIM-TSATWPPGVRRLAQS--YMKNPIqvcvgSLDLAATHSVKqIIKL 508
Cdd:cd09639 127 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEKigYVEENE-----PLDLKPNERAP-FIKI 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 509 MEDDMDKFNTITSFVKNMSSTDKIIIFCGRKVRADDLSSELTLDG--FMTQCIHGNRDQMDR----EQAIADIKSGVVRI 582
Cdd:cd09639 198 ESDKVGEISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFV 277
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21355075 583 LVATDVASRGLDIeDITHVINYDFPhnIEEYVHRVGRTGRAGR 625
Cdd:cd09639 278 IVATQVIEASLDI-SVDVMITELAP--IDSLIQRLGRLHRYGE 317
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
303-338 5.27e-05

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 46.63  E-value: 5.27e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 21355075 303 FSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLA-FL 338
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFL 58
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
526-627 1.14e-04

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 45.60  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 526 MSSTDKIIIFCGRKVRADDLSSELTLDGFMTQCIHGNRDQMDREQAIADIKSG--VVRILVATDVASRGLDIEDITHVIN 603
Cdd:COG0553 546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIH 625
                        90       100
                ....*....|....*....|....*.
gi 21355075 604 YDFPHN--IEEYvhrvgRTGRAGRQG 627
Cdd:COG0553 626 YDLWWNpaVEEQ-----AIDRAHRIG 646
KH-I_HNRNPK_rpt1 cd22432
first type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
97-141 1.47e-04

first type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411860 [Multi-domain]  Cd Length: 64  Bit Score: 40.24  E-value: 1.47e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21355075  97 IASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL---IVKITGSIQS 141
Cdd:cd22432   8 IPSKAAGAIIGKGGENIKRLRTEYNASVSVPDSSGperILTISADRET 55
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
96-138 1.86e-04

third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 40.38  E-value: 1.86e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21355075  96 SIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKC-----DLIVKITGS 138
Cdd:cd22434   7 TIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPlpgseDRIITITGT 54
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
92-141 2.73e-04

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 39.55  E-value: 2.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL-----DKCDLIVKITGSIQS 141
Cdd:cd22396   2 TEEYKVPDKMVGLIIGRGGEQINRLQAESGAKIQIapdsgGLPERPCTLTGTPDA 56
PRK13766 PRK13766
Hef nuclease; Provisional
531-625 3.81e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  531 KIIIFCGRKVRADDLSSELTLDG-----FMTQcihGNRDQMD----REQ--AIADIKSGVVRILVATDVASRGLDIEDIT 599
Cdd:PRK13766 367 RIIVFTQYRDTAEKIVDLLEKEGikavrFVGQ---ASKDGDKgmsqKEQieILDKFRAGEFNVLVSTSVAEEGLDIPSVD 443
                         90       100
                 ....*....|....*....|....*....
gi 21355075  600 HVINYD-FPHNIeEYVHRVGRTGR--AGR 625
Cdd:PRK13766 444 LVIFYEpVPSEI-RSIQRKGRTGRqeEGR 471
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
302-477 3.95e-04

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 42.24  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 302 GFSKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIhteyqstpRGTRGGANVLVLAPTreLALqieMEvKKYS 381
Cdd:cd18018   9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL--------LRRRGPGLTLVVSPL--IAL---MK-DQVD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 382 F--RGMKAVCVYGGGNRNMQISDLE--RGAE--IIICTPGRLNDLIMANVI-DVSTITYLVLDEADRMLDMG--FEP--- 449
Cdd:cd18018  75 AlpRAIKAAALNSSLTREERRRILEklRAGEvkILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWShnFRPdyl 154
                       170       180
                ....*....|....*....|....*...
gi 21355075 450 QIRKVMLDIRPDRQTIMTSATWPPGVRR 477
Cdd:cd18018 155 RLCRVLRELLGAPPVLALTATATKRVVE 182
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
93-155 4.11e-04

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 39.00  E-value: 4.11e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKcDLIVKITGSIQSNVIDAINHVRKQVT 155
Cdd:cd02393   6 TTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIED-DGTVTIFATDKESAEAAKAMIEDIVA 67
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
567-625 9.30e-04

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 40.32  E-value: 9.30e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355075 567 DREQAIADIKSGVVRILVATDVASRGLDIEDITHVINYDFPHNIEEYVHRVGRTGRAGR 625
Cdd:cd18797  80 DRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
317-441 1.16e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 40.24  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 317 LLQGHDMIGIAQ-TGTGKTL--AFLLPGMIhtEYQSTPRgtrgganVLVLAPTRELALQIEMEVKKysFRGMKAVCVYGG 393
Cdd:cd18032  16 REKGQRRALLVMaTGTGKTYtaAFLIKRLL--EANRKKR-------ILFLAHREELLEQAERSFKE--VLPDGSFGNLKG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21355075 394 GNRNMqisdleRGAEIIICTPGRLNDLIMANVIDVSTITYLVLDEADR 441
Cdd:cd18032  85 GKKKP------DDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
93-142 1.25e-03

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 37.82  E-value: 1.25e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKC------DLIVKITGSIQSN 142
Cdd:cd22457   1 QNISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAphdetgERMFTITGTPEAN 56
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
102-141 1.56e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 37.58  E-value: 1.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21355075 102 VGKVIGRGGSNISRIQNDFNVRVKL--------DKCDLIVKITGSIQS 141
Cdd:cd22437  10 CGLIIGKGGSTIKELREDSNANIKIspkdqllpGSSERIVTITGSFDQ 57
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
301-495 1.56e-03

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 40.21  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 301 MGFSKPSPIQSQAwpI--LLQGHDMIGIAQTGTGKTLAFLLPGMIHteyqstpRGTrgganVLVLAPTreLALQIEMeVK 378
Cdd:cd17920   8 FGYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALLL-------DGV-----TLVVSPL--ISLMQDQ-VD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 379 KYSFRGMKAVCVYGG---GNRNMQISDLERG-AEIIICTPGRLNDLIMANVID----VSTITYLVLDEADRMLDMG--FE 448
Cdd:cd17920  71 RLQQLGIRAAALNSTlspEEKREVLLRIKNGqYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWGhdFR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21355075 449 PQIRK--VMLDIRPDRQTIMTSATWPPGVRRLAQSY--MKNPIQVcVGSLD 495
Cdd:cd17920 151 PDYLRlgRLRRALPGVPILALTATATPEVREDILKRlgLRNPVIF-RASFD 200
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
92-148 1.83e-03

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 37.18  E-value: 1.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL---DKCDLIVKITGSiQSNVIDAIN 148
Cdd:cd22411   1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLpeeNSDSDVITITGK-KEDVEKARE 59
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
515-633 1.89e-03

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 39.54  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 515 KFNTITSFVKNMSSTDKIIIFCgrkvraDDLS-----SELTLDGFmtqcIHGNRDQMDREQAIADIKSGVVRILVATDVA 589
Cdd:cd18789  35 KLRALEELLKRHEQGDKIIVFT------DNVEalyryAKRLLKPF----ITGETPQSEREEILQNFREGEYNTLVVSKVG 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21355075 590 SRGLDIEDITHVInydfphnI--------EEYVHRVGRTGRAGRQGTSISFF 633
Cdd:cd18789 105 DEGIDLPEANVAI-------QisghggsrRQEAQRLGRILRPKKGGGKNAFF 149
KH-I_FUBP1_rpt1 cd22478
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
92-126 2.01e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411906 [Multi-domain]  Cd Length: 75  Bit Score: 37.31  E-value: 2.01e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL 126
Cdd:cd22478   5 TEEYKVPDGMVGFIIGRGGEQISRIQQESGCKIQI 39
KH_I_FMR1_FXR_rpt2 cd22426
second type I K homology (KH) RNA-binding domain found in a family of fragile X mental ...
91-137 2.26e-03

second type I K homology (KH) RNA-binding domain found in a family of fragile X mental retardation protein (FMR1) and fragile X related (FXR) proteins; The FMR1/FXR family includes FMR1 (also known as FMRP) and its two homologues, fragile X related 1 (FXR1) and 2 (FXR2). They are involved in translational regulation, particularly in neuronal cells and play an important role in the regulation of glutamate-mediated neuronal activity and plasticity. Each of these three proteins can form heteromers with the others, and each can also form homomers. Lack of expression of FMR1 results in mental retardation and macroorchidism. FXR1 and FXR2 may play important roles in the function of FMR1 and in the pathogenesis of the Fragile X Mental Retardation Syndrome. Members of this family contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411854 [Multi-domain]  Cd Length: 63  Bit Score: 36.74  E-value: 2.26e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21355075  91 FSESLSIASEMVGKVIGRGGSNISRIQNDFNVR-VKLDKCDLIVKITG 137
Cdd:cd22426   2 FIEEFKVDPDLIGLAIGSHGSNIQQARKIPGVEsIDVDEEDGTFRIYG 49
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
304-438 2.48e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 39.77  E-value: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 304 SKPSPIQSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQstpRGTRGGANVLVLAPTRELALQIEMEVKKYSFR 383
Cdd:cd18036   1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKR---RSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355075 384 GMKAVCVYGGGNRNMQISDLERGAEIIICTPGRLNDLIMANVID----VSTITYLVLDE 438
Cdd:cd18036  78 GYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
95-140 2.66e-03

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4.


Pssm-ID: 411890 [Multi-domain]  Cd Length: 66  Bit Score: 36.84  E-value: 2.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21355075  95 LSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL-----IVKITGSIQ 140
Cdd:cd22462   3 ILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSatgerIVLISGTPD 53
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
92-126 2.75e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 36.80  E-value: 2.75e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL 126
Cdd:cd22480   2 TEEYKVPDKMVGFIIGRGGEQISRIQLESGCKIQI 36
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
102-150 2.76e-03

second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 36.85  E-value: 2.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21355075 102 VGKVIGRGGSNISRIQNDFNVRVKL-DKC-----DLIVKITGSiQSNVIDAINHV 150
Cdd:cd22433  13 AGCIIGRAGFKIKELREKTGATIKVySECcprstDRVVQIGGK-PDKVVECIREI 66
ResIII pfam04851
Type III restriction enzyme, res subunit;
329-441 2.91e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.19  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075   329 TGTGKTL-AFLLPGMIHTEYQSTprgtrggaNVLVLAPTRELALQIEMEVKKYsFRGMKAVCVYGGGNRNMQISDlerGA 407
Cdd:pfam04851  32 TGSGKTLtAAKLIARLFKKGPIK--------KVLFLVPRKDLLEQALEEFKKF-LPNYVEIGEIISGDKKDESVD---DN 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 21355075   408 EIIICTPGRLNDLIMANVIDVS--TITYLVLDEADR 441
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHR 135
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
317-485 3.87e-03

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 38.94  E-value: 3.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 317 LLQGhdmigiaQTGTGKTLAFLLPgmIHTEYQStprgtrgGANVLVLAPTRELALQIEMEVKKYsFRGMKAVCVYGGGNr 396
Cdd:cd17918  40 LLSG-------DVGSGKTLVALGA--ALLAYKN-------GKQVAILVPTEILAHQHYEEARKF-LPFINVELVTGGTK- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075 397 nmqiSDLERGAEIIICTPGRLNDLIMANVIDVstityLVLDEADRmldMGFEpQIRKVMLDIRPDrqTIMTSATWPPGVR 476
Cdd:cd17918 102 ----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR---FGVA-QREALYNLGATH--FLEATATPIPRTL 166

                ....*....
gi 21355075 477 RLAQSYMKN 485
Cdd:cd17918 167 ALALSGLLD 175
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
310-370 4.30e-03

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 38.72  E-value: 4.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355075 310 QSQAWPILLQGHDMIGIAQTGTGKTLAFLLPGMIHTEYQSTPRGtrgganvLVLAPTRELA 370
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA-------LYLYPTKALA 58
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
95-150 4.77e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 36.44  E-value: 4.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075  95 LSIASEMVGKVIGRGGSNISRIQNDF--NVRV----KLDKC----DLIVKITGSIQsNVIDAINHV 150
Cdd:cd22460   4 LLVASSQAGSLIGKGGAIIKQIREESgaSVRIlpeeELPPCaspdDRVVQISGEAQ-AVKKALELV 68
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
93-154 5.72e-03

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 36.14  E-value: 5.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355075  93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKCDL-----IVKITGSiqsnvIDAINHVRKQV 154
Cdd:cd22454   6 IEVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGgspnrEVQITGS-----PDNVAAAKRLI 67
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
92-153 5.86e-03

third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 35.86  E-value: 5.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKL-DKCDLI-------VKITGSIQSnvIDAINHVRKQ 153
Cdd:cd22514   2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKIsDRGDFVsgtrnrkVTITGPQDA--VQMAQYLLEQ 69
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
92-140 8.09e-03

second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one.


Pssm-ID: 411857 [Multi-domain]  Cd Length: 82  Bit Score: 35.77  E-value: 8.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355075  92 SESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDK-------CDLIVKITGSIQ 140
Cdd:cd22429   3 TEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDResddtldLVRLITITGTKK 58
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
93-150 8.45e-03

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 39.26  E-value: 8.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21355075   93 ESLSIASEMVGKVIGRGGSNISRIQNDFNVRVKLDKcDLIVKITGSIQSNVIDAINHV 150
Cdd:PRK11824 556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIED-DGTVKIAATDGEAAEAAKERI 612
 
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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