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Conserved domains on  [gi|157819755|ref|NP_001102328|]
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DEAD-box helicase 3 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
158-408 0e+00

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: 590.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 158 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 238 SQIYTDGPGEALraMKENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                        250
                 ....*....|.
gi 157819755 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
413-543 5.91e-61

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: 199.27  E-value: 5.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 413 ITQKVVWVEEADKRSFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819755 493 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
158-408 0e+00

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: 590.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 158 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 238 SQIYTDGPGEALraMKENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                        250
                 ....*....|.
gi 157819755 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
179-566 4.10e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 484.27  E-value: 4.10e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlRAmkengky 258
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 grrkqypisLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:COG0513   75 ---------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:COG0513  146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 419 WVEEADKRSFLLDLLNATGKDSlILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:COG0513  222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157819755 499 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 566
Cdd:COG0513  301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
170-595 1.89e-131

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 397.61  E-value: 1.89e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 170 GNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQI-------YT 242
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHInaqpllrYG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 243 DGPgealramkengkygrrkqypISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATP 322
Cdd:PTZ00110 202 DGP--------------------IVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACP 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 323 GRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFL 401
Cdd:PTZ00110 262 GRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHV 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 402 AVGRVG-STSENITQKVVWVEEADKRSFLLDLLNATGKD-SLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE 479
Cdd:PTZ00110 338 NVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERT 417
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 480 EALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLV 559
Cdd:PTZ00110 418 WVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR 497
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 157819755 560 EAKQEVPSWLENMAFEHhyKGGSRGRSKsrfsGGFG 595
Cdd:PTZ00110 498 EAKQPVPPELEKLSNER--SNGTERRRW----GGYG 527
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
202-390 4.47e-61

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: 200.93  E-value: 4.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  202 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealramkengkygrrkqyPISLVLAPTRELAVQIY 281
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  282 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 157819755  362 IVEQdtMPPKgvRHTMMFSATFPKEIQML 390
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
413-543 5.91e-61

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: 199.27  E-value: 5.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 413 ITQKVVWVEEADKRSFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819755 493 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
193-416 7.17e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 7.17e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   193 IELTRYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealramkengKYGRRKQYPISLVLA 271
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755   351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 416
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
424-534 2.83e-37

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: 134.26  E-value: 2.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  424 DKRSFLLDLLNaTGKDSLILVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 503
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 157819755  504 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
453-534 2.81e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 113.85  E-value: 2.81e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   453 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 157819755   533 VG 534
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
302-556 1.53e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 95.21  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 302 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 364
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 365 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEEADKRSFLLDLLNATGK 438
Cdd:COG0514  163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 439 DSLIlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVKHVINFDLP 517
Cdd:COG0514  231 GSGI-VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157819755 518 SDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLD 556
Cdd:COG0514  309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
PRK13766 PRK13766
Hef nuclease; Provisional
429-532 7.00e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.20  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 429 LLDLLNAT---GKDSLILVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK13766 352 LREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157819755 498 VAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 532
Cdd:PRK13766 432 VAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
342-534 9.18e-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: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  342 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 421
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  422 EADKR---SFLLDLLNATGKDSLILVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 487
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157819755  488 GKSPILVATAVAARGLDISnvkhvinFDL----PSDIEEYVHRIGRTGRVG 534
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
158-408 0e+00

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: 590.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 158 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 237
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 238 SQIYTDGPGEALraMKENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 317
Cdd:cd18051   81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 318 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18051  159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                        250
                 ....*....|.
gi 157819755 398 YIFLAVGRVGS 408
Cdd:cd18051  239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
179-566 4.10e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 484.27  E-value: 4.10e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlRAmkengky 258
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 grrkqypisLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:COG0513   75 ---------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:COG0513  146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 419 WVEEADKRSFLLDLLNATGKDSlILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:COG0513  222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157819755 499 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 566
Cdd:COG0513  301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
179-407 2.54e-161

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: 461.96  E-value: 2.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealramkENGKY 258
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP--------PSVGR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:cd17967   73 GRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 339 CKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVG 407
Cdd:cd17967  153 IKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
137-407 7.41e-152

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: 439.40  E-value: 7.41e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 137 PLPPSERlEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKR 216
Cdd:cd18052    3 PPPPPED-EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 217 DLMACAQTGSGKTAAFLLPILSQIYTDGpgeaLRAMKENGKygrrkQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPC 296
Cdd:cd18052   82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSEV-----QEPQALIVAPTRELANQIFLEARKFSYGTCIRPV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 297 VVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHT 376
Cdd:cd18052  153 VVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQT 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157819755 377 MMFSATFPKEIQMLARDFLDE-YIFLAVGRVG 407
Cdd:cd18052  233 LMFSATFPEEIQRLAAEFLKEdYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
170-595 1.89e-131

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 397.61  E-value: 1.89e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 170 GNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQI-------YT 242
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHInaqpllrYG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 243 DGPgealramkengkygrrkqypISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATP 322
Cdd:PTZ00110 202 DGP--------------------IVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACP 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 323 GRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFL 401
Cdd:PTZ00110 262 GRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHV 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 402 AVGRVG-STSENITQKVVWVEEADKRSFLLDLLNATGKD-SLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE 479
Cdd:PTZ00110 338 NVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERT 417
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 480 EALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLV 559
Cdd:PTZ00110 418 WVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR 497
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 157819755 560 EAKQEVPSWLENMAFEHhyKGGSRGRSKsrfsGGFG 595
Cdd:PTZ00110 498 EAKQPVPPELEKLSNER--SNGTERRRW----GGYG 527
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
198-546 1.24e-97

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 307.50  E-value: 1.24e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealramkeNGKYgRRKQypiSLVLAPTRELA 277
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQ---ALVLCPTRELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKFSyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:PRK11776  86 DQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYifLAVgRVGSTSEN--ITQKVVWVEEADKRSF 428
Cdd:PRK11776 160 LDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 429 LLDLLNATGKDSlILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 508
Cdd:PRK11776 233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 157819755 509 KHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNER 546
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
179-566 1.70e-96

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 304.42  E-value: 1.70e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealramkeNGKy 258
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP---------HAK- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 GRRkqyPI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:PRK10590  72 GRR---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 417
Cdd:PRK10590 149 QVEILVLDEADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 418 VWVEEADKRSfLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK10590 225 HFVDKKRKRE-LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATD 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 498 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 566
Cdd:PRK10590 304 IAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
189-401 1.04e-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: 292.81  E-value: 1.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealramkengkygRRKQYPISL 268
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK--------------KKGRGPQAL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd00268   67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157819755 349 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd00268  147 RMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
164-589 5.78e-92

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 294.39  E-value: 5.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 164 IPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILS---QI 240
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 241 YTDGPGEalramkengkygRRKqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA 320
Cdd:PLN00206 187 RSGHPSE------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVG 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 321 TPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgvrHTMMFSATFPKEIQMLARDFLDEYIF 400
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIIL 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 401 LAVGRVGSTSENITQKVVWVEEADKRSFLLDLLNATGK-DSLILVFVETKKGADSLEDFL-YHEGYACTSIHGDRSQRDR 478
Cdd:PLN00206 328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHfKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKER 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 479 EEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLL 558
Cdd:PLN00206 408 REVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL 487
                        410       420       430
                 ....*....|....*....|....*....|.
gi 157819755 559 VEAKQEVPSWLENmafeHHYKGGSRGRSKSR 589
Cdd:PLN00206 488 KSSGAAIPRELAN----SRYLGSGRKRKKKR 514
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
180-545 1.10e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 289.89  E-value: 1.10e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 180 FSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIyTDGPGEALRAMKEngkyg 259
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQL-LQTPPPKERYMGE----- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 260 rrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:PRK01297 163 -----PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDM 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 339 CKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 418
Cdd:PRK01297 238 VEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVY 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 419 WVEEADKRSFLLDLLNATGKDSlILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 498
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWER-VMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 157819755 499 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNE 545
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
189-401 3.80e-83

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: 260.38  E-value: 3.80e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIyTDGPgealramkengkYGRRKQYPISL 268
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQP------------PLERGDGPIVL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17966   68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157819755 349 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17966  148 RMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
180-542 4.49e-83

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 268.35  E-value: 4.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 180 FSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsQIYTDGPgealramkengkyg 259
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 260 RRKQYPIS-LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 338
Cdd:PRK11192  68 RRKSGPPRiLILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 339 CKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGVRHTMMFSATFPKE-IQMLARDFLDEYIFLAVGrvGSTSE--NITQ 415
Cdd:PRK11192 148 VETLILDEADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQ 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 416 kvvWVEEAD----KRSFLLDLLNATGKDSLIlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP 491
Cdd:PRK11192 222 ---WYYRADdlehKTALLCHLLKQPEVTRSI-VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVN 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819755 492 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 542
Cdd:PRK11192 298 VLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
179-567 3.30e-81

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 267.97  E-value: 3.30e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgPGEAlramkengky 258
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI-GLD 337
Cdd:PRK04537  79 DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 417
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 418 VWVEEADKRSFLLDLLNATgKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK04537 237 YFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 498 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERninITKDLLDLLVEAKQEVPS 567
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIPV 382
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
202-542 5.81e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 257.21  E-value: 5.81e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 202 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEalramkengkyGRRKQYPISLVLAPTRELAVQIY 281
Cdd:PRK04837  32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE-----------DRKVNQPRALIMAPTRELAVQIH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 282 EEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 362 IVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEEADKRSFLLDLLNATGKDSL 441
Cdd:PRK04837 181 LFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 442 IlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIE 521
Cdd:PRK04837 259 I-IFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCE 337
                        330       340
                 ....*....|....*....|.
gi 157819755 522 EYVHRIGRTGRVGNLGLATSF 542
Cdd:PRK04837 338 DYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
179-546 2.63e-71

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 242.83  E-value: 2.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLRAmkengky 258
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:PRK11634  75 ------PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 417
Cdd:PRK11634 149 KLSGLVLDEADEMLRMGFIEDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 418 VWVEEADKRSFLLDLLNATGKDSLIlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK11634 225 WTVWGMRKNEALVRFLEAEDFDAAI-IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATD 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 498 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNER 546
Cdd:PRK11634 304 VAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENR 352
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
168-395 1.31e-70

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: 228.42  E-value: 1.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 168 ATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGE 247
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 248 AlramkENGkygrrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVD 327
Cdd:cd17953   82 P-----GEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMID 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 328 M--MERGKI-GLDFCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17953  149 IltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRPD--RQTVLFSATFPRKVEALARKVL 215
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
166-404 1.41e-69

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: 226.04  E-value: 1.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 166 VEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgp 245
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 246 gealramkENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 325
Cdd:cd18049   87 --------NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 326 VDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd18049  159 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
170-404 6.16e-68

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: 223.35  E-value: 6.16e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 170 GNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeal 249
Cdd:cd18050   54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 250 ramkENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 329
Cdd:cd18050  125 ----NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157819755 330 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd18050  201 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
189-399 8.67e-67

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: 217.28  E-value: 8.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealraMKEngKYGRRKQYPISL 268
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-----------MDQ--RELEKGEGPIAV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17952   68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819755 349 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYI 399
Cdd:cd17952  148 RMFDMGFEYQVRSIVGH-VRPD---RQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
193-395 7.36e-64

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: 210.64  E-value: 7.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 193 IELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealrAMKENGKYGrrkqyPISLVLAP 272
Cdd:cd17945    5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPP-----LDEETKDDG-----PYALILAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 273 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 352
Cdd:cd17945   75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 353 MGFEPQIRRIVeqDTMPP------------------KGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17945  155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
PTZ00424 PTZ00424
helicase 45; Provisional
177-554 9.54e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 216.23  E-value: 9.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 177 IESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLRAMKeng 256
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD-----LNACQ--- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 257 kygrrkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 336
Cdd:PTZ00424  99 ----------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 337 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQK 416
Cdd:PTZ00424 169 DDLKLFILDEADEMLSRGFKGQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQF 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 417 VVWVEEAD-KRSFLLDLLNATGKDSLIlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVA 495
Cdd:PTZ00424 245 YVAVEKEEwKFDTLCDLYETLTITQAI-IYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLIT 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 496 TAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDL 554
Cdd:PTZ00424 324 TDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
202-390 4.47e-61

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: 200.93  E-value: 4.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  202 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealramkengkygrrkqyPISLVLAPTRELAVQIY 281
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  282 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 361
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 157819755  362 IVEQdtMPPKgvRHTMMFSATFPKEIQML 390
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
413-543 5.91e-61

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: 199.27  E-value: 5.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 413 ITQKVVWVEEADKRSFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 492
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819755 493 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
197-392 1.70e-57

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: 193.18  E-value: 1.70e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 197 RYTRPTPVQKHAI-PIIKEKRDLMACAQTGSGKTAAFLLPilsqiytdgpgeALRAMKENGKYGRRKQYPIsLVLAPTRE 275
Cdd:cd17964   13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNTKPAGRRSGVSA-LIISPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 276 LAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDFCKYLVLDEADRML 351
Cdd:cd17964   80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157819755 352 DMGFEPQIRRIVeqDTMPPKGVRH--TMMFSATFPKEIQMLAR 392
Cdd:cd17964  160 DMGFRPDLEQIL--RHLPEKNADPrqTLLFSATVPDEVQQIAR 200
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
189-404 1.79e-57

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: 192.80  E-value: 1.79e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALRAmkengkygrrkqypisL 268
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------L 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 347
Cdd:cd17957   65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157819755 348 DRMLDMGFEPQIRRIVEQDTMPPKgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVG 404
Cdd:cd17957  145 DKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEXDc smart00487
DEAD-like helicases superfamily;
193-416 7.17e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 7.17e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   193 IELTRYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealramkengKYGRRKQYPISLVLA 271
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755   351 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 416
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
198-396 7.67e-57

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: 190.93  E-value: 7.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQ-IYTDGPGEALRAmkengkygrrkqypisLVLAPTREL 276
Cdd:cd17947   10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRPKKKAATRV----------------LVLVPTREL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 277 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGF 355
Cdd:cd17947   74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157819755 356 EPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLARDFLD 396
Cdd:cd17947  154 ADELKEILR---LCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
189-397 2.22e-55

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: 186.90  E-value: 2.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqIYTDgpgealramKENGKYGRRKQyPISL 268
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLD---------LQPIPREQRNG-PGVL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKFSYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 348
Cdd:cd17958   69 VLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 349 RMLDMGFEPQIRRIVeQDTMPPkgvRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd17958  148 RMLDMGFEPQIRKIL-LDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
198-400 6.68e-55

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: 185.89  E-value: 6.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGpgealramkengkYGrrkqyPISLVLAPTRELA 277
Cdd:cd17955   19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP-------------YG-----IFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDFCKYLVLDEADRMLDMG 354
Cdd:cd17955   81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157819755 355 FEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIF 400
Cdd:cd17955  161 FEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
200-395 6.24e-54

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: 183.69  E-value: 6.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 200 RPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgeaLRAMKENGKYG-RRKQYPISLVLAPTRELAV 278
Cdd:cd17951   12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-----------MFALEQEKKLPfIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 279 QIYEEARKFSYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 352
Cdd:cd17951   81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157819755 353 MGFEPQIRRIVEQDtmppKGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17951  161 MGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
179-392 9.14e-53

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: 180.21  E-value: 9.14e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 179 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealramkengky 258
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 grrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLD 337
Cdd:cd17954   66 ---PQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLK 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157819755 338 FCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPKgvRHTMMFSATFPKEIQMLAR 392
Cdd:cd17954  143 SLKFLVMDEADRLLNMDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
197-401 1.26e-48

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: 169.30  E-value: 1.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 197 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPgealRAMKENGKYGrrkqypisLVLAPTREL 276
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP----RVDRSDGTLA--------LVLVPTREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 277 AVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMG 354
Cdd:cd17949   78 ALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755 355 FEPQIRRIVE--------QDTMPPKGV-RHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17949  158 FEKDITKILEllddkrskAGGEKSKPSrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
187-399 1.88e-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: 168.63  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 187 EIIMGNIELTrYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGealramkengkygrrkqypI 266
Cdd:cd17940    9 ELLMGIFEKG-FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV-------------------I 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 267 -SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLD 345
Cdd:cd17940   69 qALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLD 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157819755 346 EADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQmlarDFLDEYI 399
Cdd:cd17940  149 EADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
198-401 1.03e-47

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: 166.71  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALRAmkengkygrrkqypisLVLAPTRELA 277
Cdd:cd17959   21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARA----------------LILSPTRELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEP 357
Cdd:cd17959   85 LQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAE 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157819755 358 QIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 401
Cdd:cd17959  165 QLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
198-395 1.29e-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: 166.21  E-value: 1.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYtdgpgealramkeNGKYGRRKQYPISLVLAPTRELA 277
Cdd:cd17960   10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-------------KRKANLKKGQVGALIISPTRELA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKF--SYRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDEADRMLD 352
Cdd:cd17960   77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157819755 353 MGFEPQIRRIVEQdtmPPKGvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17960  157 LGFEADLNRILSK---LPKQ-RRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
198-403 6.59e-45

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: 158.61  E-value: 6.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIY------TDGPGealramkengkygrrkqypiSLVLA 271
Cdd:cd17941   10 FIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG--------------------ALIIS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 272 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDF--CKYLVLDEA 347
Cdd:cd17941   70 PTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEA 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755 348 DRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAV 403
Cdd:cd17941  146 DRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
184-382 1.77e-44

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: 157.87  E-value: 1.77e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 184 EMG---EIIMGnIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealramkengkygr 260
Cdd:cd17938    3 ELGvmpELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 261 rkQYPISLVLAPTRELAVQIYEEARKFSY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 337
Cdd:cd17938   59 --QIVVALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLS 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 338 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVR----HTMMFSAT 382
Cdd:cd17938  137 SVRFFVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
192-399 4.86e-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: 156.17  E-value: 4.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 192 NIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSqiytdgpgealRAMKEngkygrrKQYPISLVLA 271
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII-----------RCLTE-------HRNPSALILT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 272 PTRELAVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 350
Cdd:cd17962   66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 351 LDMGFEPQIRRIVEQDTMPPKgvrhTMMFSATFPKEIQMLARDFLDEYI 399
Cdd:cd17962  146 LKMGFQQQVLDILENISHDHQ----TILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
197-392 1.15e-41

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: 151.24  E-value: 1.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 197 RYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLRAMKENGKYGRRKqYPISLVLAPTRE 275
Cdd:cd17946    9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKSSNGVGGKQK-PLRALILTPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 276 LAVQI---YEEARKFsyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DFCKYLVLDEADR 349
Cdd:cd17946   80 LAVQVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157819755 350 MLDMG-FEP--QIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLAR 392
Cdd:cd17946  157 MLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLK 202
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
189-392 3.63e-41

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: 148.66  E-value: 3.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 189 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgeaLRAMKENGKYGrrkqypisL 268
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK------LKFKPRNGTGV--------I 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 269 VLAPTRELAVQIYEEARKF-SYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiglDF----CKYLV 343
Cdd:cd17942   67 IISPTRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK---GFlyknLQCLI 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 344 LDEADRMLDMGFEPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLAR 392
Cdd:cd17942  143 IDEADRILEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
198-395 4.42e-40

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: 145.80  E-value: 4.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgeaLRAMKENGKYgrrkQYPISLVLAPTRELA 277
Cdd:cd17961   14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEE----QGTRALILVPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKFSY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DFCKYLVLDEADRMLDM 353
Cdd:cd17961   82 QQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157819755 354 GFEPQIRRIVEqdtMPPKGVRHTMMfSATFPKEIQMLARDFL 395
Cdd:cd17961  161 GYEEDLKSLLS---YLPKNYQTFLM-SATLSEDVEALKKLVL 198
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
198-395 2.37e-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: 140.54  E-value: 2.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLRAMKengkygrrkqypiSLVLAPTREL 276
Cdd:cd17939   17 FEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDTT-----VRETQ-------------ALVLAPTREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 277 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 354
Cdd:cd17939   78 AQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157819755 355 FEPQIRRIVeqdTMPPKGVRhTMMFSATFPKEIQMLARDFL 395
Cdd:cd17939  156 FKDQIYDIF---QFLPPETQ-VVLFSATMPHEVLEVTKKFM 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
198-394 4.65e-38

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: 139.63  E-value: 4.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealramkengkygrRKQYPISLVLAPTRE 275
Cdd:cd17963   14 FNKPSKIQETALPLIlsDPPENLIAQSQSGTGKTAAFVLAMLSRVDP------------------TLKSPQALCLAPTRE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 276 LAVQIYEEARKF-SY-----RSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 349
Cdd:cd17963   76 LARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157819755 350 MLDM-GFEPQIRRIVEqdtMPPKGVRhTMMFSATFPKEIQMLARDF 394
Cdd:cd17963  147 MLDTqGHGDQSIRIKR---MLPRNCQ-ILLFSATFPDSVRKFAEKI 188
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
424-534 2.83e-37

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: 134.26  E-value: 2.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  424 DKRSFLLDLLNaTGKDSLILVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 503
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 157819755  504 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
180-395 2.27e-35

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: 132.57  E-value: 2.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 180 FSDVEMGEIIMGNIELTRYTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgeaLRAMKengky 258
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIK-GYDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQ----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 259 grrkqypiSLVLAPTRELAVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 336
Cdd:cd18046   70 --------ALVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRT 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 337 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd18046  140 DYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFM 194
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
201-395 3.44e-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: 132.08  E-value: 3.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 201 PTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgPGEalramkengkygrrkqypIS-LVLAPTRELAVQ 279
Cdd:cd17950   25 PSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPV-DGQ------------------VSvLVICHTRELAFQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 280 IYEEARKFS-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM---LDMg 354
Cdd:cd17950   86 ISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLDM- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157819755 355 fepqiRRIVeQD--TMPPKGvRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17950  165 -----RRDV-QEifRATPHD-KQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
198-400 3.74e-34

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: 128.54  E-value: 3.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALRamkengkygRRKQYPISLVLAPTRELA 277
Cdd:cd17943   10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL---------ESLD---------LERRHPQVLILAPTREIA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 278 VQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 356
Cdd:cd17943   72 VQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157819755 357 PQIRRIveqDTMPPKGvRHTMMFSATFPKE-IQMLARdFLDEYIF 400
Cdd:cd17943  151 KDVNWI---FSSLPKN-KQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
198-397 1.31e-30

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: 119.11  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 198 YTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYTdgpgealrAMKEngkygrrkqyPISLVLAPTREL 276
Cdd:cd18045   19 FEKPSAIQQRAIkPIIK-GRDVIAQSQSGTGKTATFSISVLQCLDI--------QVRE----------TQALILSPTREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 277 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 356
Cdd:cd18045   80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157819755 357 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDE 397
Cdd:cd18045  160 EQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
203-395 2.66e-30

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: 118.03  E-value: 2.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 203 PVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgEALRAMKENGKYGRRkqyPISLVLAPTRELAVQIYE 282
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLI---------EKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 283 EARKFSYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRI 362
Cdd:cd17944   83 DFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 157819755 363 V-EQDTMPPKGVRHTMMFSATFPKEIQMLARDFL 395
Cdd:cd17944  161 LsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
HELICc smart00490
helicase superfamily c-terminal domain;
453-534 2.81e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 113.85  E-value: 2.81e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755   453 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 157819755   533 VG 534
Cdd:smart00490  81 AG 82
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
195-385 1.81e-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: 116.70  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 195 LTRY--TRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealramKENGkyGRRKQYPISLVLAP 272
Cdd:cd17948    5 LQRQgiTKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRY---------KLLA--EGPFNAPRGLVITP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 273 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRML 351
Cdd:cd17948   74 SRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157819755 352 DMGFEPQIRRIVEQ-----------DTMPPKGvrHTMMFSATFPK 385
Cdd:cd17948  153 DDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPS 195
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
197-390 6.36e-27

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: 109.26  E-value: 6.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 197 RYTRPTPVQKHAIP-IIKE--------KRDLMACAQTGSGKTAAFLLPILsQIYTDGPGEALRAmkengkygrrkqypis 267
Cdd:cd17956    9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 268 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-IGLDF 338
Cdd:cd17956   72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKH 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 339 CKYLVLDEADRMLDMGFE---PQIRRIVEQDTMP------------PKGVR-HTMMFSATF---PKEIQML 390
Cdd:cd17956  152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPdlgsfgdanlleRSVRPlQKLLFSATLtrdPEKLSSL 222
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
185-394 5.63e-24

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: 101.30  E-value: 5.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 185 MGEIIMGNIELTRYTRPTPVQKHAIPII------KEKRD-----------LMAcAQTGSGKTAAFLLPILSQIYTD--GP 245
Cdd:cd17965   15 IKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrKVTKQtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQeqEP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 246 GEALRAMKEN-GKYGRrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVATP 322
Cdd:cd17965   94 FEEAEEEYESaKDTGR----PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTTP 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157819755 323 GRLVDMME-RGKIgLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgVRHTMMFSATFPKEIQMLARDF 394
Cdd:cd17965  170 GKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
213-529 1.35e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 98.94  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 213 KEKRDLMACAQTGSGKTAAfllpilsqiytdgpgeALRAMKENGKYGRrkqypiSLVLAPTRELAVQIYEEARKFsyrsr 292
Cdd:COG1061   98 RGGGRGLVVAPTGTGKTVL----------------ALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF----- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 293 vrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDFCKYLVLDEADRmldmGFEPQIRRIVEQdtMPPKg 372
Cdd:COG1061  151 ------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 373 vrHTMMFSAT------FPKEI-------------QMLARDFLDEYIFLAV--------GRVGSTSENITQKVVWVEEAdK 425
Cdd:COG1061  215 --YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALAADAER-K 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 426 RSFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 505
Cdd:COG1061  292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
                        330       340
                 ....*....|....*....|....
gi 157819755 506 SNVKHVINFDLPSDIEEYVHRIGR 529
Cdd:COG1061  372 PRLDVAILLRPTGSPREFIQRLGR 395
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
302-556 1.53e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 95.21  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 302 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 364
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 365 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEEADKRSFLLDLLNATGK 438
Cdd:COG0514  163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 439 DSLIlVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVKHVINFDLP 517
Cdd:COG0514  231 GSGI-VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157819755 518 SDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLD 556
Cdd:COG0514  309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
177-391 1.92e-18

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: 84.69  E-value: 1.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 177 IESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealramke 254
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLSRV-------------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 255 ngkyGRRKQYPISLVLAPTRELAVQ---IYEEARKFSYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPGRLVD 327
Cdd:cd18048   83 ----DALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPGTVLD 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755 328 MMERGK-IGLDFCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPKGvrHTMMFSATFPKEIQMLA 391
Cdd:cd18048  150 WCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
420-532 2.93e-15

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 79.39  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 420 VEEAD----KRSFLLDLLN---ATGKDSLILVFVETKKGADSLEDFLYHEGYACT------SIHGDR--SQRDREEALHQ 484
Cdd:COG1111  327 AEEADiehpKLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILER 406
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157819755 485 FRSGKSPILVATAVAARGLDISNVKHVINFDL-PSDIeEYVHRIGRTGR 532
Cdd:COG1111  407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
429-529 8.64e-14

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: 68.77  E-value: 8.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 429 LLDLLNAT---GKDSLILVFVETKKGADSLEDFLYHEGYACTSI-------HGDRSQ--------RDREEALHQFRSGKS 490
Cdd:cd18802   12 LIEILREYfpkTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQrkrslmtqRKQKETLDKFRDGEL 91
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157819755 491 PILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 529
Cdd:cd18802   92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
178-391 1.26e-13

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: 70.13  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 178 ESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSQIytdGPGealramken 255
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV---EPA--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 256 gkygrrKQYPISLVLAPTRELAVQ---IYEEARKFSyrsrvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLVDM 328
Cdd:cd18047   69 ------NKYPQCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDW 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157819755 329 MERGK-IGLDFCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGVRhTMMFSATFPKEIQMLA 391
Cdd:cd18047  134 CSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNCQ-MLLFSATFEDSVWKFA 194
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
220-382 1.43e-13

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: 68.58  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 220 ACAQTGSGKTAAFLLPILSQIYTDGPGealramkengkygrrkqypiSLVLAPTRELAVQIYEEARK-FSYRSRVRpcVV 298
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKKGKK--------------------VLVLVPTKALALQTAERLRElFGPGIRVA--VL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 299 YGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpPKGVRhTM 377
Cdd:cd00046   64 VGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG-LKNAQ-VI 141

                 ....*
gi 157819755 378 MFSAT 382
Cdd:cd00046  142 LLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
426-528 7.64e-13

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: 65.96  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 426 RSFLLDLLNATGKdslILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGL 503
Cdd:cd18793   17 LELLEELREPGEK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGL 93
                         90       100       110
                 ....*....|....*....|....*....|.
gi 157819755 504 DISNVKHVINFDL---PSDIE---EYVHRIG 528
Cdd:cd18793   94 NLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
420-534 8.43e-12

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: 63.00  E-value: 8.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 420 VEEADKRSFLLDLLNATGKDSL---ILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVAT 496
Cdd:cd18794    8 VRPKDKKDEKLDLLKRIKVEHLggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157819755 497 AVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:cd18794   88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
PRK13766 PRK13766
Hef nuclease; Provisional
429-532 7.00e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.20  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 429 LLDLLNAT---GKDSLILVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATA 497
Cdd:PRK13766 352 LREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157819755 498 VAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 532
Cdd:PRK13766 432 VAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
433-532 1.07e-09

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: 57.37  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 433 LNATGKDSLILVFVETKKGADSLEDFLYHE----------GYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARG 502
Cdd:cd18801   24 KKQEGSDTRVIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEG 103
                         90       100       110
                 ....*....|....*....|....*....|.
gi 157819755 503 LDISNVKHVINFD-LPSDIeEYVHRIGRTGR 532
Cdd:cd18801  104 LDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
199-539 1.08e-09

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: 61.78  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 199 TRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEAlramkengkygrrkqypisLVLAPTRELAV 278
Cdd:COG1205   55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------------------LYLYPTKALAR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 279 QIYEEARKF--SYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERgkiGL--------DF---CKYLV 343
Cdd:COG1205  116 DQLRRLRELaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHY---GLlphhtrwaRFfrnLRYVV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 344 LDEA---------------DRMldmgfepqiRRIVEQdtmppKGVRHTMMF-SATF--PKEiqmLARDFLDEYiFLAVGR 405
Cdd:COG1205  186 IDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP-VTVVDE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 406 VGSTSENITQkVVW----VEEADKRSFLLD----LLNATGKDSLILVFVETKKGA----DSLEDFLYHEGYAcTSIHGDR 473
Cdd:COG1205  248 DGSPRGERTF-VLWnpplVDDGIRRSALAEaarlLADLVREGLRTLVFTRSRRGAellaRYARRALREPDLA-DRVAAYR 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 474 SQ---RDREEALHQFRSGKSPILVAT-AVAArGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLA 539
Cdd:COG1205  326 AGylpEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
416-533 1.11e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.39  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 416 KVVWVEEadkrsFLLDLLNATGKdslILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--IL 493
Cdd:COG0553  534 KLEALLE-----LLEELLAEGEK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFL 605
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157819755 494 VATAVAARGLDISNVKHVINFDLP--SDIEEY----VHRIGRTGRV 533
Cdd:COG0553  606 ISLKAGGEGLNLTAADHVIHYDLWwnPAVEEQaidrAHRIGQTRDV 651
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
202-347 1.41e-08

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 57.60  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 202 TPVQKHAIP-IIKEKRDLMACAQTGSGKTAafllpiLSQIYtdgpgeALRAMKENGKygrrkqypiSLVLAPTRELAVQI 280
Cdd:COG1204   24 YPPQAEALEaGLLEGKNLVVSAPTASGKTL------IAELA------ILKALLNGGK---------ALYIVPLRALASEK 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 281 YEEARKFSYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIGL--DFcKYLVLDEA 347
Cdd:COG1204   83 YREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSWlrDV-DLVVVDEA 146
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
200-382 1.72e-08

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: 54.73  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 200 RPTPVQKHAIPII------KEKRDLMACAQTGSGKTAAFLLPILsqiytdgpgealrAMKENGKYgrrkqypiSLVLAPT 273
Cdd:cd17918   15 SLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGAAL-------------LAYKNGKQ--------VAILVPT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 274 RELAVQIYEEARKfsYRSRVRPCVVYGG--ADIGQQIrDLERGCHLLVAtpgrlvdmMERGKIGLDFckyLVLDEADRMl 351
Cdd:cd17918   74 EILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-SLLVGTHALLH--------LDVKFKNLDL---VIVDEQHRF- 138
                        170       180       190
                 ....*....|....*....|....*....|.
gi 157819755 352 dmgfepqirRIVEQDTMPPKGVRHTMMFSAT 382
Cdd:cd17918  139 ---------GVAQREALYNLGATHFLEATAT 160
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
492-532 2.06e-08

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: 51.55  E-value: 2.06e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 157819755 492 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 532
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
197-250 1.67e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.72  E-value: 1.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157819755 197 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKT-AAFlLPILSQIYTDGPGEALR 250
Cdd:COG1201   21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
205-347 3.60e-07

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: 50.66  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 205 QKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDgpgealramkengkYGRRkqypiSLVLAPTRELAVQIYEEA 284
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD--------------PGSR-----ALYLYPTKALAQDQLRSL 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157819755 285 RKF--SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDFC---KYLVLDEA 347
Cdd:cd17923   66 RELleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLrnlRYVVLDEA 134
PRK13767 PRK13767
ATP-dependent helicase; Provisional
197-322 9.96e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 52.20  E-value: 9.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 197 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALramkENGKYgrrkqypiSLVLAPTREL 276
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL----EDKVY--------CLYVSPLRAL 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157819755 277 A-----------VQIYEEARKFSYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 322
Cdd:PRK13767  97 NndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
215-347 1.10e-06

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: 49.57  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 215 KRDLMACAQTGSGKT--AAFLLPILSQIytdgpgeaLRAMKENGKygrrkqypISLVLAPTRELAVQIYEEARKFSYrSR 292
Cdd:cd18034   16 KRNTIVVLPTGSGKTliAVMLIKEMGEL--------NRKEKNPKK--------RAVFLVPTVPLVAQQAEAIRSHTD-LK 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157819755 293 VRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 347
Cdd:cd18034   79 VGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
202-347 1.48e-06

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: 48.80  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 202 TPVQKHAI-PIIKEKRDLMACAQTGSGKTAAFLLPIlsqiytdgpgeaLRAMKENGKygrrkqypISLVLAPTRELAVQI 280
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAI------------LRALATSGG--------KAVYIAPTRALVNQK 62
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157819755 281 YEEARKFSYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLVDMMERGKIGLDF-CKYLVLDEA 347
Cdd:cd17921   63 EADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEA 127
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
206-383 3.13e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.30  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 206 KHAIPIIKEKRDLMACAQTGSGKTAAfllpilsqiytdgpgeALRAMKEngkygrRKQYPIsLVLAPTRELAVQIYEEAR 285
Cdd:cd17926    9 LEAWLAHKNNRRGILVLPTGSGKTLT----------------ALALIAY------LKELRT-LIVVPTDALLDQWKERFE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 286 KFSYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRmldmGFEPQIRRIVEQ 365
Cdd:cd17926   66 DFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKE 133
                        170
                 ....*....|....*...
gi 157819755 366 DTMPPKgvrhtMMFSATF 383
Cdd:cd17926  134 LNAKYR-----LGLTATP 146
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
342-534 9.18e-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: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  342 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 421
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  422 EADKR---SFLLDLLNATGKDSLILVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 487
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157819755  488 GKSPILVATAVAARGLDISnvkhvinFDL----PSDIEEYVHRIGRTGRVG 534
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
460-534 1.47e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.09  E-value: 1.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819755 460 YHEGYactsihgDRSQRDR-EEAlhqFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 534
Cdd:PRK11057 266 YHAGL-------DNDVRADvQEA---FQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
428-543 1.56e-04

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: 42.62  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 428 FLLDLLNATGKdslILVFVETKKGADSL-EDFLYhegYActsIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI- 505
Cdd:cd18789   41 ELLKRHEQGDK---IIVFTDNVEALYRYaKRLLK---PF---ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLp 111
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157819755 506 -SNVKHVINFDLPSDiEEYVHRIGRTGRVGNLGLATSFF 543
Cdd:cd18789  112 eANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
469-534 1.62e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 42.33  E-value: 1.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 534
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
215-349 3.27e-04

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: 42.12  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 215 KRDLMACAQTGSGKTAAFLLPILSqiytdgpgealRAMKENGKYgrrkqypisLVLAPTRELAVQIYEEARKFsyRSRVR 294
Cdd:cd18035   16 NGNTLIVLPTGLGKTIIAILVAAD-----------RLTKKGGKV---------LILAPSRPLVEQHAENLKRV--LNIPD 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157819755 295 PCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 349
Cdd:cd18035   74 KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
443-532 4.75e-04

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: 41.10  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 443 LVFVETKKGADSLED---FLYHEGYACTSI---HG--DRSQRDR-EEALhqfRSGKSPILVATAVAARGLDISNVKHVIN 513
Cdd:cd18796   42 LVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVIQ 118
                         90
                 ....*....|....*....
gi 157819755 514 FDLPSDIEEYVHRIGRTGR 532
Cdd:cd18796  119 IGSPKSVARLLQRLGRSGH 137
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
468-577 9.20e-04

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 42.60  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  468 SIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFFNER 546
Cdd:PRK09751  306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                          90       100       110
                  ....*....|....*....|....*....|.
gi 157819755  547 NiniTKDLLDLLVEAKQEVPSWLENMAFEHH 577
Cdd:PRK09751  384 T---RRDLVDSAVIVECMFAGRLENLTPPHN 411
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
420-533 1.02e-03

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 42.48  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755  420 VEEADKRSFLLDLL-NATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR---SGKSPILVA 495
Cdd:PLN03142  467 VENSGKMVLLDKLLpKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLS 546
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 157819755  496 TAVAARGLDISNVKHVINFDlpSD--------IEEYVHRIGRTGRV 533
Cdd:PLN03142  547 TRAGGLGINLATADIVILYD--SDwnpqvdlqAQDRAHRIGQKKEV 590
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
469-534 1.13e-03

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 39.94  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 534
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
443-529 1.55e-03

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 38.69  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 443 LVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE-EALHQFRSGKS--PILVATAVAARGLDISNVKHVInFDLP-- 517
Cdd:cd18799   10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRPte 88
                         90
                 ....*....|..
gi 157819755 518 SDIeEYVHRIGR 529
Cdd:cd18799   89 SRT-LFLQMLGR 99
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
216-346 1.61e-03

DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.87  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 216 RDLMACAQTGSGKTAAFLLPILSQIYtDGPGEALRAMkengkYgrrkqypISlvlaPTRELAVQIYE------EARKFSY 289
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQVL-----Y-------IS----PLKALINDQERrleeplDEIDLEI 64
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819755 290 RSRVRpcvvYGgaDIGQQIRD--LERGCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDE 346
Cdd:cd17922   65 PVAVR----HG--DTSQSEKAkqLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDE 119
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
342-556 1.66e-03

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: 41.26  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 342 LVLDEADrmldmGFEPQIRRIVEQ--DTMPPKGVRHTMMfSATFPKeiqmlardFLDEYiFLAVGRV----GSTSENITQ 415
Cdd:cd09639  127 LIFDEVH-----FYDEYTLALILAvlEVLKDNDVPILLM-SATLPK--------FLKEY-AEKIGYVeenePLDLKPNER 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 416 KVVWVEEADKR---SFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSI--HGDRSQRDR----EEALHQFR 486
Cdd:cd09639  192 APFIKIESDKVgeiSSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFK 271
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157819755 487 SGKSPILVATAVAARGLDISnvkhvinFDL----PSDIEEYVHRIGRTGRVGnlglatsFFNERNINITKDLLD 556
Cdd:cd09639  272 KSEKFVIVATQVIEASLDIS-------VDVmiteLAPIDSLIQRLGRLHRYG-------EKNGEEVYIITDAPD 331
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
469-532 3.43e-03

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 38.48  E-value: 3.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 469 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN-----VKHVINFDLPSdieeyVHRI-GRTGR 532
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR 131
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
204-331 3.46e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 39.26  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 204 VQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILSQIytdgpgealraMKENGKY-GRRKqypiSLVLAPTRELAVQIY 281
Cdd:cd18023    5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAILRLL-----------KERNPLPwGNRK----VVYIAPIKALCSEKY 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157819755 282 EEAR-KFsyrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 331
Cdd:cd18023   70 DDWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
442-532 9.63e-03

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 37.61  E-value: 9.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819755 442 ILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDlpSDIE 521
Cdd:cd18790   30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107
                         90
                 ....*....|....*...
gi 157819755 522 EY-------VHRIGRTGR 532
Cdd:cd18790  108 GFlrsetslIQTIGRAAR 125
 
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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